CA1341617C - Inhibin isolated from ovarian follicular fluid - Google Patents
Inhibin isolated from ovarian follicular fluidInfo
- Publication number
- CA1341617C CA1341617C CA482470A CA482470A CA1341617C CA 1341617 C CA1341617 C CA 1341617C CA 482470 A CA482470 A CA 482470A CA 482470 A CA482470 A CA 482470A CA 1341617 C CA1341617 C CA 1341617C
- Authority
- CA
- Canada
- Prior art keywords
- inhibin
- protein
- mammal
- antiserum
- sub
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 239000000893 inhibin Substances 0.000 title claims abstract description 157
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 title claims abstract description 156
- 210000001733 follicular fluid Anatomy 0.000 title claims abstract description 22
- 230000002611 ovarian Effects 0.000 title claims abstract description 16
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 55
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 55
- 238000000034 method Methods 0.000 claims abstract description 54
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 claims abstract description 43
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 claims abstract description 43
- 229940028334 follicle stimulating hormone Drugs 0.000 claims abstract description 43
- 238000000338 in vitro Methods 0.000 claims abstract description 20
- 238000010828 elution Methods 0.000 claims abstract description 19
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 claims abstract description 19
- 238000004007 reversed phase HPLC Methods 0.000 claims abstract description 18
- 238000005227 gel permeation chromatography Methods 0.000 claims abstract description 16
- 238000004166 bioassay Methods 0.000 claims abstract description 15
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims abstract description 15
- 230000002710 gonadal effect Effects 0.000 claims abstract description 13
- 238000003127 radioimmunoassay Methods 0.000 claims abstract description 13
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims abstract description 10
- 229940088597 hormone Drugs 0.000 claims abstract description 9
- 239000005556 hormone Substances 0.000 claims abstract description 9
- 230000001592 luteinising effect Effects 0.000 claims abstract description 7
- 102000003946 Prolactin Human genes 0.000 claims abstract description 4
- 108010057464 Prolactin Proteins 0.000 claims abstract description 4
- 229920002684 Sepharose Polymers 0.000 claims abstract description 4
- 102000011923 Thyrotropin Human genes 0.000 claims abstract description 4
- 108010061174 Thyrotropin Proteins 0.000 claims abstract description 4
- 229940097325 prolactin Drugs 0.000 claims abstract description 4
- HBOMLICNUCNMMY-KJFJCRTCSA-N 1-[(4s,5s)-4-azido-5-(hydroxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione Chemical compound O=C1NC(=O)C(C)=CN1C1O[C@H](CO)[C@@H](N=[N+]=[N-])C1 HBOMLICNUCNMMY-KJFJCRTCSA-N 0.000 claims abstract description 3
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 claims abstract description 3
- 229910052740 iodine Inorganic materials 0.000 claims abstract description 3
- 239000011630 iodine Substances 0.000 claims abstract description 3
- 230000002285 radioactive effect Effects 0.000 claims abstract description 3
- 102000002746 Inhibins Human genes 0.000 claims description 150
- 108010004250 Inhibins Proteins 0.000 claims description 150
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 46
- 230000000694 effects Effects 0.000 claims description 29
- 241000124008 Mammalia Species 0.000 claims description 24
- 239000000463 material Substances 0.000 claims description 21
- 241000283690 Bos taurus Species 0.000 claims description 16
- 230000003053 immunization Effects 0.000 claims description 15
- 238000004519 manufacturing process Methods 0.000 claims description 13
- 230000016087 ovulation Effects 0.000 claims description 13
- 239000012149 elution buffer Substances 0.000 claims description 10
- 239000000872 buffer Substances 0.000 claims description 9
- 239000012506 Sephacryl® Substances 0.000 claims description 8
- 229920005654 Sephadex Polymers 0.000 claims description 8
- 239000012507 Sephadex™ Substances 0.000 claims description 8
- 150000001413 amino acids Chemical class 0.000 claims description 7
- 210000004027 cell Anatomy 0.000 claims description 7
- 102000003886 Glycoproteins Human genes 0.000 claims description 6
- 108090000288 Glycoproteins Proteins 0.000 claims description 6
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 6
- 239000002671 adjuvant Substances 0.000 claims description 5
- 238000001556 precipitation Methods 0.000 claims description 5
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 5
- 239000007858 starting material Substances 0.000 claims description 5
- 101100228210 Caenorhabditis elegans gly-7 gene Proteins 0.000 claims description 4
- 230000035558 fertility Effects 0.000 claims description 4
- 239000012634 fragment Substances 0.000 claims description 4
- 239000011800 void material Substances 0.000 claims description 4
- AUXMWYRZQPIXCC-KNIFDHDWSA-N (2s)-2-amino-4-methylpentanoic acid;(2s)-2-aminopropanoic acid Chemical compound C[C@H](N)C(O)=O.CC(C)C[C@H](N)C(O)=O AUXMWYRZQPIXCC-KNIFDHDWSA-N 0.000 claims description 3
- 101100436100 Caenorhabditis elegans asp-6 gene Proteins 0.000 claims description 3
- IMTUWVJPCQPJEE-IUCAKERBSA-N Met-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN IMTUWVJPCQPJEE-IUCAKERBSA-N 0.000 claims description 3
- GLUBLISJVJFHQS-VIFPVBQESA-N Phe-Gly Chemical compound OC(=O)CNC(=O)[C@@H](N)CC1=CC=CC=C1 GLUBLISJVJFHQS-VIFPVBQESA-N 0.000 claims description 3
- 239000004698 Polyethylene Substances 0.000 claims description 3
- RVQDZELMXZRSSI-IUCAKERBSA-N Pro-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 RVQDZELMXZRSSI-IUCAKERBSA-N 0.000 claims description 3
- UPJONISHZRADBH-XPUUQOCRSA-N Val-Glu Chemical compound CC(C)[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O UPJONISHZRADBH-XPUUQOCRSA-N 0.000 claims description 3
- 239000000427 antigen Substances 0.000 claims description 3
- 108091007433 antigens Proteins 0.000 claims description 3
- 102000036639 antigens Human genes 0.000 claims description 3
- 238000000502 dialysis Methods 0.000 claims description 3
- 230000001817 pituitary effect Effects 0.000 claims description 3
- -1 polyethylene Polymers 0.000 claims description 3
- 229920000573 polyethylene Polymers 0.000 claims description 3
- 230000009467 reduction Effects 0.000 claims description 3
- 238000002791 soaking Methods 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 2
- 102000004190 Enzymes Human genes 0.000 claims description 2
- 239000003480 eluent Substances 0.000 claims description 2
- 230000002401 inhibitory effect Effects 0.000 claims description 2
- 230000000977 initiatory effect Effects 0.000 claims description 2
- 229920002401 polyacrylamide Polymers 0.000 claims description 2
- 239000000377 silicon dioxide Substances 0.000 claims description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 2
- 235000018102 proteins Nutrition 0.000 claims 26
- 239000000203 mixture Substances 0.000 claims 11
- 230000001225 therapeutic effect Effects 0.000 claims 5
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 3
- 235000001014 amino acid Nutrition 0.000 claims 3
- 235000009582 asparagine Nutrition 0.000 claims 3
- 150000001508 asparagines Chemical class 0.000 claims 3
- 235000003704 aspartic acid Nutrition 0.000 claims 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 3
- 239000003085 diluting agent Substances 0.000 claims 3
- 229920001184 polypeptide Polymers 0.000 claims 3
- FYYSIASRLDJUNP-WHFBIAKZSA-N Glu-Asp Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(O)=O FYYSIASRLDJUNP-WHFBIAKZSA-N 0.000 claims 2
- 102000009151 Luteinizing Hormone Human genes 0.000 claims 2
- 108010073521 Luteinizing Hormone Proteins 0.000 claims 2
- 239000002253 acid Substances 0.000 claims 2
- 230000003111 delayed effect Effects 0.000 claims 2
- 239000003937 drug carrier Substances 0.000 claims 2
- 239000000839 emulsion Substances 0.000 claims 2
- 108010063718 gamma-glutamylaspartic acid Proteins 0.000 claims 2
- 229940040129 luteinizing hormone Drugs 0.000 claims 2
- 230000001568 sexual effect Effects 0.000 claims 2
- XUUXCWCKKCZEAW-YFKPBYRVSA-N Arg-Gly Chemical compound OC(=O)CNC(=O)[C@@H](N)CCCN=C(N)N XUUXCWCKKCZEAW-YFKPBYRVSA-N 0.000 claims 1
- PBSQFBAJKPLRJY-BYULHYEWSA-N Asn-Gly-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)CNC(=O)[C@H](CC(=O)N)N PBSQFBAJKPLRJY-BYULHYEWSA-N 0.000 claims 1
- 101100015199 Caenorhabditis elegans gly-11 gene Proteins 0.000 claims 1
- 101100228206 Caenorhabditis elegans gly-6 gene Proteins 0.000 claims 1
- 238000002965 ELISA Methods 0.000 claims 1
- CUPSDFQZTVVTSK-GUBZILKMSA-N Glu-Lys-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCC(O)=O CUPSDFQZTVVTSK-GUBZILKMSA-N 0.000 claims 1
- UFPXDFOYHVEIPI-BYPYZUCNSA-N Gly-Gly-Asp Chemical compound NCC(=O)NCC(=O)N[C@H](C(O)=O)CC(O)=O UFPXDFOYHVEIPI-BYPYZUCNSA-N 0.000 claims 1
- 239000003433 contraceptive agent Substances 0.000 claims 1
- 230000002254 contraceptive effect Effects 0.000 claims 1
- 238000002405 diagnostic procedure Methods 0.000 claims 1
- 230000001804 emulsifying effect Effects 0.000 claims 1
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 claims 1
- 239000011159 matrix material Substances 0.000 claims 1
- 230000021595 spermatogenesis Effects 0.000 claims 1
- 238000005406 washing Methods 0.000 claims 1
- 238000000746 purification Methods 0.000 abstract description 17
- 238000001727 in vivo Methods 0.000 abstract description 6
- 238000012512 characterization method Methods 0.000 abstract description 4
- 239000013014 purified material Substances 0.000 abstract description 4
- 108010001267 Protein Subunits Proteins 0.000 abstract description 2
- 239000000499 gel Substances 0.000 description 17
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 15
- 229960000583 acetic acid Drugs 0.000 description 15
- 238000002360 preparation method Methods 0.000 description 14
- 241001465754 Metazoa Species 0.000 description 13
- 238000002649 immunization Methods 0.000 description 12
- 239000000523 sample Substances 0.000 description 12
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 11
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 11
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 241000283973 Oryctolagus cuniculus Species 0.000 description 9
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 9
- 230000006870 function Effects 0.000 description 8
- 210000002966 serum Anatomy 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- 238000002523 gelfiltration Methods 0.000 description 7
- 230000002829 reductive effect Effects 0.000 description 7
- 230000000638 stimulation Effects 0.000 description 7
- 230000002381 testicular Effects 0.000 description 7
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 6
- 239000005695 Ammonium acetate Substances 0.000 description 6
- 229940043376 ammonium acetate Drugs 0.000 description 6
- 235000019257 ammonium acetate Nutrition 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000011084 recovery Methods 0.000 description 6
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 5
- 235000012538 ammonium bicarbonate Nutrition 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 210000001672 ovary Anatomy 0.000 description 5
- 239000002904 solvent Substances 0.000 description 5
- 230000001629 suppression Effects 0.000 description 5
- 210000001550 testis Anatomy 0.000 description 5
- 241000700159 Rattus Species 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 238000011068 loading method Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000003472 neutralizing effect Effects 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108090001090 Lectins Proteins 0.000 description 3
- 102000004856 Lectins Human genes 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 239000002523 lectin Substances 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 2
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- 239000004160 Ammonium persulphate Substances 0.000 description 2
- 208000002109 Argyria Diseases 0.000 description 2
- BBBXWRGITSUJPB-YUMQZZPRSA-N Glu-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CCC(O)=O BBBXWRGITSUJPB-YUMQZZPRSA-N 0.000 description 2
- SCCPDJAQCXWPTF-VKHMYHEASA-N Gly-Asp Chemical compound NCC(=O)N[C@H](C(O)=O)CC(O)=O SCCPDJAQCXWPTF-VKHMYHEASA-N 0.000 description 2
- KGVHCTWYMPWEGN-FSPLSTOPSA-N Gly-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)CN KGVHCTWYMPWEGN-FSPLSTOPSA-N 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- ROOXNKNUYICQNP-UHFFFAOYSA-N ammonium persulfate Chemical compound [NH4+].[NH4+].[O-]S(=O)(=O)OOS([O-])(=O)=O ROOXNKNUYICQNP-UHFFFAOYSA-N 0.000 description 2
- 235000019395 ammonium persulphate Nutrition 0.000 description 2
- 239000003708 ampul Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 2
- 238000006073 displacement reaction Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 230000008217 follicular development Effects 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 239000012362 glacial acetic acid Substances 0.000 description 2
- 210000002149 gonad Anatomy 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 231100000546 inhibition of ovulation Toxicity 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- ZIUHHBKFKCYYJD-UHFFFAOYSA-N n,n'-methylenebisacrylamide Chemical compound C=CC(=O)NCNC(=O)C=C ZIUHHBKFKCYYJD-UHFFFAOYSA-N 0.000 description 2
- 210000002381 plasma Anatomy 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000008141 pubertal development Effects 0.000 description 2
- 239000000700 radioactive tracer Substances 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- KYRUKRFVOACELK-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(4-hydroxyphenyl)propanoate Chemical compound C1=CC(O)=CC=C1CCC(=O)ON1C(=O)CCC1=O KYRUKRFVOACELK-UHFFFAOYSA-N 0.000 description 1
- DGZSVBBLLGZHSF-UHFFFAOYSA-N 4,4-diethylpiperidine Chemical compound CCC1(CC)CCNCC1 DGZSVBBLLGZHSF-UHFFFAOYSA-N 0.000 description 1
- ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 1
- 229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 1
- 241000272814 Anser sp. Species 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101100228200 Caenorhabditis elegans gly-5 gene Proteins 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 244000304337 Cuminum cyminum Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 206010062767 Hypophysitis Diseases 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 206010033165 Ovarian failure Diseases 0.000 description 1
- RQTDRJMAUKHGHV-UHFFFAOYSA-N P.P.I Chemical compound P.P.I RQTDRJMAUKHGHV-UHFFFAOYSA-N 0.000 description 1
- UJTZHGHXJKIAOS-WHFBIAKZSA-N Ser-Gln Chemical compound OC[C@H](N)C(=O)N[C@H](C(O)=O)CCC(N)=O UJTZHGHXJKIAOS-WHFBIAKZSA-N 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 108010046516 Wheat Germ Agglutinins Proteins 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000001099 ammonium carbonate Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000003610 charcoal Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 description 1
- 229960004407 chorionic gonadotrophin Drugs 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 210000002196 fr. b Anatomy 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 210000002503 granulosa cell Anatomy 0.000 description 1
- 108010021083 hen egg lysozyme Proteins 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 108010067471 inhibin A Proteins 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 201000004535 ovarian dysfunction Diseases 0.000 description 1
- 231100000539 ovarian failure Toxicity 0.000 description 1
- 210000003101 oviduct Anatomy 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 210000003635 pituitary gland Anatomy 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 208000006155 precocious puberty Diseases 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 210000002863 seminiferous tubule Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 235000011008 sodium phosphates Nutrition 0.000 description 1
- GNBVPFITFYNRCN-UHFFFAOYSA-M sodium thioglycolate Chemical compound [Na+].[O-]C(=O)CS GNBVPFITFYNRCN-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000003637 steroidlike Effects 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229960001479 tosylchloramide sodium Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 229940108519 trasylol Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/689—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to pregnancy or the gonads
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/26—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against hormones ; against hormone releasing or inhibiting factors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/815—Test for named compound or class of compounds
- Y10S436/817—Steroids or hormones
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/806—Antigenic peptides or proteins
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/85—Reproductive organs or embryos
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Genetics & Genomics (AREA)
- Urology & Nephrology (AREA)
- Endocrinology (AREA)
- Biophysics (AREA)
- General Physics & Mathematics (AREA)
- Toxicology (AREA)
- Cell Biology (AREA)
- Reproductive Health (AREA)
- Microbiology (AREA)
- Pregnancy & Childbirth (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Gynecology & Obstetrics (AREA)
- Pathology (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Steroid Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- External Artificial Organs (AREA)
- Centrifugal Separators (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AUPG542784 | 1984-06-08 | ||
| AUPG5427 | 1984-06-08 | ||
| AUPH00031 | 1985-04-04 | ||
| AUPH003185 | 1985-04-04 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1341617C true CA1341617C (en) | 2011-06-28 |
Family
ID=25642809
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA482470A Expired - Fee Related CA1341617C (en) | 1984-06-08 | 1985-05-27 | Inhibin isolated from ovarian follicular fluid |
Country Status (10)
| Country | Link |
|---|---|
| US (2) | US5102807A (cg-RX-API-DMAC7.html) |
| EP (1) | EP0185034B1 (cg-RX-API-DMAC7.html) |
| JP (2) | JP2521707B2 (cg-RX-API-DMAC7.html) |
| AT (1) | ATE95194T1 (cg-RX-API-DMAC7.html) |
| CA (1) | CA1341617C (cg-RX-API-DMAC7.html) |
| DE (1) | DE3587603T2 (cg-RX-API-DMAC7.html) |
| DK (1) | DK171711B1 (cg-RX-API-DMAC7.html) |
| NO (1) | NO176570C (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ212248A (cg-RX-API-DMAC7.html) |
| WO (1) | WO1986000078A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1341617C (en) * | 1984-06-08 | 2011-06-28 | Henry George Burger | Inhibin isolated from ovarian follicular fluid |
| EP0218717B1 (en) * | 1985-04-18 | 1998-07-15 | Biotechnology Australia Pty. Ltd. | Recombinant inhibin |
| US5089396A (en) * | 1985-10-03 | 1992-02-18 | Genentech, Inc. | Nucleic acid encoding β chain prodomains of inhibin and method for synthesizing polypeptides using such nucleic acid |
| US5215893A (en) * | 1985-10-03 | 1993-06-01 | Genentech, Inc. | Nucleic acid encoding the ba chain prodomains of inhibin and method for synthesizing polypeptides using such nucleic acid |
| US4798885A (en) * | 1986-02-07 | 1989-01-17 | Genentech, Inc. | Compositions of hormonally active human and porcine inhibin containing an α chain and 62 chain |
| NZ217727A (en) * | 1985-10-03 | 1990-05-28 | Genentech Inc | Nucleic acid encoding alpha or b chain of inhibin, its production and compositions containing it |
| US4864019A (en) * | 1985-11-08 | 1989-09-05 | The Salk Institute For Biological Studies | Antibodies to inhibin and conjugates produced therefrom |
| IL81889A0 (en) * | 1986-03-13 | 1987-10-20 | Biotech Australia Pty Ltd | Assay of inhibin |
| US5015729A (en) * | 1986-06-24 | 1991-05-14 | The Salk Institute For Biological Studies | Ovine inhibin |
| US6150328A (en) * | 1986-07-01 | 2000-11-21 | Genetics Institute, Inc. | BMP products |
| JP2802633B2 (ja) * | 1987-01-29 | 1998-09-24 | バイオテクノロジー・オーストラリア・プロプライエタリー・リミテツド | たん白 |
| US5032507A (en) * | 1987-11-13 | 1991-07-16 | The Salk Institute For Biological Studies | Potentiation of erythropoiesis |
| US5196192A (en) * | 1988-05-31 | 1993-03-23 | Biotechnology Australia Pty. Ltd. | Actions of hormones |
| DE4042408C2 (de) * | 1990-01-08 | 1995-04-06 | Stefan Heiden | Verwendung von Inhibin- neutralisierenden Antikörpern |
| DE69105114T2 (de) * | 1990-01-08 | 1995-05-04 | Genentech Inc | Methode zur erhöhung der fruchtbarkeit weiblicher säuger. |
| US5942220A (en) * | 1990-03-16 | 1999-08-24 | Chiron Corporation | Inhibitor of cytokine activity and applications thereof |
| JP3504263B2 (ja) * | 1991-11-04 | 2004-03-08 | ジェネティックス・インスチチュート・リミテッド・ライアビリティ・カンパニー | 組み換え型骨形態形成蛋白ヘテロダイマー、組成物および使用法 |
| US20080070842A1 (en) * | 1991-11-04 | 2008-03-20 | David Israel | Recombinant bone morphogenetic protein heterodimers, compositions and methods of use |
| US5428011A (en) * | 1992-06-16 | 1995-06-27 | Procyon Biopharma, Inc. | Pharmaceutical preparations for inhibiting tumours associated with prostate adenocarcinoma |
| KR100227406B1 (ko) | 1993-05-12 | 1999-12-01 | 브루스 엠. 에이센 | Bmp-11 조성물 |
| US6291206B1 (en) * | 1993-09-17 | 2001-09-18 | Genetics Institute, Inc. | BMP receptor proteins |
| JP3717930B2 (ja) | 1993-12-07 | 2005-11-16 | ジェネティックス・インスチチュート・リミテッド・ライアビリティ・カンパニー | Ｂｍｐ−１２、ｂｍｐ−１３およびそれらの腱誘導組成物 |
| US5786179A (en) * | 1994-02-28 | 1998-07-28 | Agritech Technologies Ltd. | Heterologous protein comprising avian alpha-subunit inhibin protein and methods of producing same |
| US5747659A (en) * | 1994-02-28 | 1998-05-05 | Agritech Technologies, Ltd. | Fusion gene products encoding avian alpha subunit inhibin protein, or an immunogenic fragment thereof, and a carrier protein |
| US20030171283A1 (en) * | 1994-02-28 | 2003-09-11 | Satterlee Daniel G. | Inhibin compositions and methods of enhancing production performance |
| AUPO638897A0 (en) * | 1997-04-23 | 1997-05-22 | Monash University | Modulation of cell growth and methods relating thereto |
| AU780982B2 (en) * | 1997-04-23 | 2005-04-28 | Monash University | Inhibin modulation of cell growth |
| TW586934B (en) * | 1997-05-19 | 2004-05-11 | Sumitomo Pharma | Immunopotentiating composition |
| US6727224B1 (en) * | 1999-02-01 | 2004-04-27 | Genetics Institute, Llc. | Methods and compositions for healing and repair of articular cartilage |
| CA2386408A1 (en) | 1999-10-15 | 2001-04-26 | Genetics Institute, Inc. | Formulations of hyaluronic acid for delivery of osteogenic proteins |
| CA2355334A1 (en) * | 2000-10-16 | 2002-04-16 | Procyon Biopharma Inc. | Pharmaceutical preparations and methods for inhibiting tumors |
| US20030082233A1 (en) * | 2000-12-01 | 2003-05-01 | Lyons Karen M. | Method and composition for modulating bone growth |
| TWI329129B (en) * | 2001-02-08 | 2010-08-21 | Wyeth Corp | Modified and stabilized gdf propeptides and uses thereof |
| EP1399023B1 (en) * | 2001-06-01 | 2008-04-30 | Wyeth | COMPOSITIONS FOR SYSTEMIC ADMINISTRATION OF SEQUENCES ENCODING BONE MORPHOGENETIC PROTEINS& x9; |
| TWI267378B (en) * | 2001-06-08 | 2006-12-01 | Wyeth Corp | Calcium phosphate delivery vehicles for osteoinductive proteins |
| US20050026833A1 (en) * | 2001-11-08 | 2005-02-03 | Rabbani Shafaat Ahmed | PSP-94: use for treatment of hypercalcemia and bone metastasis |
| CA2486113A1 (en) * | 2002-05-17 | 2003-12-04 | Wyeth | Injectable solid hyaluronic acid carriers for delivery of osteogenic proteins |
| WO2004043287A2 (en) * | 2002-11-07 | 2004-05-27 | Agritech Technology, Ltd | Novel compositions that enhance production performance in avians |
| CN1878565B (zh) * | 2003-09-12 | 2011-01-12 | 惠氏公司 | 用于递送成骨蛋白的注射型磷酸钙固体小棒剂和糊剂 |
| WO2012074870A2 (en) | 2010-11-29 | 2012-06-07 | Mote Marine Laboratory, Inc. | Fish sexual characteristic determination using peptide hormones |
| BR102014005376A2 (pt) * | 2014-03-07 | 2016-02-10 | Ouro Fino Saúde Animal Ltda | antígeno de inibina alfa, gene codificante de inibina alfa, gene codificante de proteína de fusão, processo de obtenção do antígeno de inibina alfa, composição antigênica, uso do antígeno de inibina alfa e uso da composição antigênica |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1007568A (en) * | 1973-12-13 | 1977-03-29 | Michael C. Attwell | Bovine immunoglobulin isolation process |
| FR2361912A1 (fr) * | 1976-08-19 | 1978-03-17 | Merck & Co Inc | Vaccin anti-fecondite a base de membrane pellucide solubilisee |
| US4409139A (en) * | 1981-08-10 | 1983-10-11 | The Salk Institute For Biological Studies | Gonadostatin |
| US4423037A (en) * | 1982-05-13 | 1983-12-27 | The General Hospital Corporation | Inhibitors of peptide hormone action |
| CA1341617C (en) * | 1984-06-08 | 2011-06-28 | Henry George Burger | Inhibin isolated from ovarian follicular fluid |
| EP0218717B1 (en) * | 1985-04-18 | 1998-07-15 | Biotechnology Australia Pty. Ltd. | Recombinant inhibin |
| US4624944A (en) * | 1985-06-14 | 1986-11-25 | The Regents Of The University Of California | Human seminal alpha-inhibins |
| US4740587A (en) * | 1985-07-18 | 1988-04-26 | The Salk Institute For Biological Studies | Inhibin and method of purifying same |
| US4798885A (en) * | 1986-02-07 | 1989-01-17 | Genentech, Inc. | Compositions of hormonally active human and porcine inhibin containing an α chain and 62 chain |
| US4864019A (en) * | 1985-11-08 | 1989-09-05 | The Salk Institute For Biological Studies | Antibodies to inhibin and conjugates produced therefrom |
| US4737578A (en) * | 1986-02-10 | 1988-04-12 | The Salk Institute For Biological Studies | Human inhibin |
| US5196192A (en) * | 1988-05-31 | 1993-03-23 | Biotechnology Australia Pty. Ltd. | Actions of hormones |
-
1985
- 1985-05-27 CA CA482470A patent/CA1341617C/en not_active Expired - Fee Related
- 1985-05-30 NZ NZ212248A patent/NZ212248A/en unknown
- 1985-06-03 WO PCT/AU1985/000119 patent/WO1986000078A1/en not_active Ceased
- 1985-06-03 AT AT85902422T patent/ATE95194T1/de not_active IP Right Cessation
- 1985-06-03 JP JP60502564A patent/JP2521707B2/ja not_active Expired - Lifetime
- 1985-06-03 EP EP85902422A patent/EP0185034B1/en not_active Expired - Lifetime
- 1985-06-03 DE DE85902422T patent/DE3587603T2/de not_active Expired - Lifetime
-
1986
- 1986-02-06 NO NO860427A patent/NO176570C/no unknown
- 1986-02-07 DK DK060586A patent/DK171711B1/da not_active IP Right Cessation
-
1989
- 1989-04-11 US US07/336,053 patent/US5102807A/en not_active Expired - Lifetime
- 1989-08-03 US US07/389,328 patent/US5364837A/en not_active Expired - Lifetime
-
1995
- 1995-03-06 JP JP7084463A patent/JP2583030B2/ja not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| DK60586D0 (da) | 1986-02-07 |
| WO1986000078A1 (en) | 1986-01-03 |
| DK60586A (da) | 1986-02-07 |
| NZ212248A (en) | 1991-05-28 |
| DE3587603D1 (de) | 1993-11-04 |
| JPH0848636A (ja) | 1996-02-20 |
| NO176570C (no) | 1995-04-26 |
| US5364837A (en) | 1994-11-15 |
| NO860427L (no) | 1986-02-06 |
| US5102807A (en) | 1992-04-07 |
| DK171711B1 (da) | 1997-04-01 |
| JP2583030B2 (ja) | 1997-02-19 |
| EP0185034A4 (cg-RX-API-DMAC7.html) | 1988-01-28 |
| EP0185034A1 (cg-RX-API-DMAC7.html) | 1986-06-25 |
| NO176570B (no) | 1995-01-16 |
| ATE95194T1 (de) | 1993-10-15 |
| EP0185034B1 (en) | 1993-09-29 |
| JPS61502399A (ja) | 1986-10-23 |
| JP2521707B2 (ja) | 1996-08-07 |
| DE3587603T2 (de) | 1994-02-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA1341617C (en) | Inhibin isolated from ovarian follicular fluid | |
| Lewis et al. | Human prolactin: isolation and some properties | |
| Cornell et al. | The subunits of human pituitary thyroid-stimulating hormone: isolation, properties, and composition | |
| Shome et al. | Human and porcine thyrotropins: a comparison of electrophoretic and immunological properties with the bovine hormone | |
| GB2268179A (en) | Antibodies to purified HCG receptors | |
| Berghman et al. | Glycosylated chicken growth hormone | |
| EP0260306A1 (en) | Method of assay of inhibin | |
| YAMAGUCHI et al. | Simultaneous determination of human plasma immunoreactive β-lipotropin, γ-lipotropin, and β-endorphin using immune-affinity chromatography | |
| US4966888A (en) | hCG-hLH receptor and hCG-hLH receptor-hCG complex as antigens, antibodies thereto and contraceptive vaccine | |
| CA1057742A (en) | Antigenic modification of polypeptides | |
| AU636318B2 (en) | Inhibin isolated from ovarian follicular fluid | |
| IE63385B1 (en) | A method for the selective immunological determination of intact procollagen peptide (Type III) and procollagen (Type III) in body fluids and means for carrying it out | |
| Birken et al. | Preparation and analysis of the common urinary forms of human chorionic gonadotropin | |
| Papkoff et al. | Pituitary growth hormone from the turtle and duck: purification and immunochemical studies | |
| Reddy et al. | Purification and some properties of ovine placental lactogen | |
| MacKenzie et al. | Purification of thyrotropin from the pituitaries of two turtles: the green sea turtle and the snapping turtle | |
| Weiss et al. | Partial purification of relaxin from human seminal plasma | |
| CA1305829C (en) | Ovine inhibin | |
| WHITLEY et al. | Studies on the isolation and chemical-physical properties of porcine follicle-stimulating hormone | |
| EP0000103A1 (en) | Purification of glycoproteins and use of glycoproteins to form antiserum compositions | |
| US4271069A (en) | Beta-hCG preparation and method | |
| Hellema | The chameleonic behaviour of gonadotrophins: A review of recent results on their physicochemical properties and molecular structure | |
| Vandewalle et al. | Further characterization of the light breast cyst fluid protein, GCDFP-15 | |
| Desplan et al. | Isolation of circulating immunoreactive human parathyroid hormone: comparison with a 1-34 N-terminal synthetic fragment | |
| CHEN et al. | Immunological studies of the follicle-stimulating hormone. I. Identification of the HCG augmenting principle |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MKLA | Lapsed |
Effective date: 20210628 |