SE454299B - Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptiden - Google Patents
Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptidenInfo
- Publication number
- SE454299B SE454299B SE8604270A SE8604270A SE454299B SE 454299 B SE454299 B SE 454299B SE 8604270 A SE8604270 A SE 8604270A SE 8604270 A SE8604270 A SE 8604270A SE 454299 B SE454299 B SE 454299B
- Authority
- SE
- Sweden
- Prior art keywords
- iapp
- amino acid
- ser
- human
- polypeptide
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title description 20
- 102000004196 processed proteins & peptides Human genes 0.000 title description 10
- 229920001184 polypeptide Polymers 0.000 title description 8
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 claims abstract description 71
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 claims abstract description 71
- PLOPBXQQPZYQFA-AXPWDRQUSA-N amlintide Chemical compound C([C@@H](C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)CSSC1)[C@@H](C)O)C(C)C)C1=CC=CC=C1 PLOPBXQQPZYQFA-AXPWDRQUSA-N 0.000 claims abstract description 71
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 18
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 18
- 238000002360 preparation method Methods 0.000 claims description 24
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 18
- 241000282414 Homo sapiens Species 0.000 claims description 17
- 230000000984 immunochemical effect Effects 0.000 claims description 6
- 239000003547 immunosorbent Substances 0.000 claims description 5
- 238000012549 training Methods 0.000 claims description 3
- 239000002994 raw material Substances 0.000 claims description 2
- 108020003175 receptors Proteins 0.000 claims description 2
- 102000005962 receptors Human genes 0.000 claims description 2
- 210000004153 islets of langerhan Anatomy 0.000 abstract description 15
- 239000000463 material Substances 0.000 abstract description 5
- 108010014497 Islet Amyloid Polypeptide Receptors Proteins 0.000 abstract 1
- 241000282326 Felis catus Species 0.000 description 21
- 235000001014 amino acid Nutrition 0.000 description 20
- 150000001413 amino acids Chemical class 0.000 description 17
- 238000000034 method Methods 0.000 description 16
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 12
- 235000018102 proteins Nutrition 0.000 description 12
- 206010022498 insulinoma Diseases 0.000 description 11
- 208000021255 pancreatic insulinoma Diseases 0.000 description 11
- 239000000126 substance Substances 0.000 description 9
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 9
- 101100286193 Homo sapiens IAPP gene Proteins 0.000 description 8
- 102000004877 Insulin Human genes 0.000 description 7
- 108090001061 Insulin Proteins 0.000 description 7
- 125000000539 amino acid group Chemical group 0.000 description 7
- 241000282412 Homo Species 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 206010012601 diabetes mellitus Diseases 0.000 description 6
- 238000004128 high performance liquid chromatography Methods 0.000 description 6
- 229940125396 insulin Drugs 0.000 description 6
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 102000001049 Amyloid Human genes 0.000 description 5
- 108010094108 Amyloid Proteins 0.000 description 5
- 206010028980 Neoplasm Diseases 0.000 description 5
- 210000000227 basophil cell of anterior lobe of hypophysis Anatomy 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 239000007790 solid phase Substances 0.000 description 5
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000007812 deficiency Effects 0.000 description 4
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 4
- 102100038518 Calcitonin Human genes 0.000 description 3
- 108090000932 Calcitonin Gene-Related Peptide Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 3
- 239000012736 aqueous medium Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 235000019253 formic acid Nutrition 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 229960004198 guanidine Drugs 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 210000000496 pancreas Anatomy 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 239000012071 phase Substances 0.000 description 3
- 239000002504 physiological saline solution Substances 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 208000037259 Amyloid Plaque Diseases 0.000 description 2
- 102000055006 Calcitonin Human genes 0.000 description 2
- 108060001064 Calcitonin Proteins 0.000 description 2
- 241000700199 Cavia porcellus Species 0.000 description 2
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 2
- 102000002067 Protein Subunits Human genes 0.000 description 2
- 108010001267 Protein Subunits Proteins 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 238000005903 acid hydrolysis reaction Methods 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 2
- 229960004015 calcitonin Drugs 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- DNKYDHSONDSTNJ-XJVRLEFXSA-N chembl1910953 Chemical compound C([C@@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CS)NC(=O)[C@H](C)N)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)C1=CN=CN1 DNKYDHSONDSTNJ-XJVRLEFXSA-N 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- IQFVPQOLBLOTPF-HKXUKFGYSA-L congo red Chemical compound [Na+].[Na+].C1=CC=CC2=C(N)C(/N=N/C3=CC=C(C=C3)C3=CC=C(C=C3)/N=N/C3=C(C4=CC=CC=C4C(=C3)S([O-])(=O)=O)N)=CC(S([O-])(=O)=O)=C21 IQFVPQOLBLOTPF-HKXUKFGYSA-L 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 230000002055 immunohistochemical effect Effects 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 201000002528 pancreatic cancer Diseases 0.000 description 2
- 230000008506 pathogenesis Effects 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 239000000376 reactant Substances 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- HFDKKNHCYWNNNQ-YOGANYHLSA-N 75976-10-2 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)N)C(C)C)[C@@H](C)O)C1=CC=C(O)C=C1 HFDKKNHCYWNNNQ-YOGANYHLSA-N 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 241000282324 Felis Species 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 101000983116 Homo sapiens Pancreatic prohormone Proteins 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 108010048233 Procalcitonin Proteins 0.000 description 1
- 208000017442 Retinal disease Diseases 0.000 description 1
- 206010038923 Retinopathy Diseases 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000004520 agglutination Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 125000004057 biotinyl group Chemical group [H]N1C(=O)N([H])[C@]2([H])[C@@]([H])(SC([H])([H])[C@]12[H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C(*)=O 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- WORJEOGGNQDSOE-UHFFFAOYSA-N chloroform;methanol Chemical compound OC.ClC(Cl)Cl WORJEOGGNQDSOE-UHFFFAOYSA-N 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 210000000609 ganglia Anatomy 0.000 description 1
- 230000000574 ganglionic effect Effects 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 108091008039 hormone receptors Proteins 0.000 description 1
- 102000046327 human PPY Human genes 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 238000012151 immunohistochemical method Methods 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 230000000366 juvenile effect Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 208000023356 medullary thyroid gland carcinoma Diseases 0.000 description 1
- 150000002734 metacrylic acid derivatives Chemical class 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 230000036963 noncompetitive effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000010003 pancreatic endocrine function Effects 0.000 description 1
- 210000004923 pancreatic tissue Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- -1 poly (hydroxyalkyl acrylates Chemical class 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 108010066381 preproinsulin Proteins 0.000 description 1
- CWCXERYKLSEGEZ-KDKHKZEGSA-N procalcitonin Chemical compound C([C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(O)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCSC)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@@H](N)CSSC1)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 CWCXERYKLSEGEZ-KDKHKZEGSA-N 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000013818 thyroid gland medullary carcinoma Diseases 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
- G01N33/57407—Specifically defined cancers
- G01N33/57438—Specifically defined cancers of liver, pancreas or kidney
-
- 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
- G01N33/6893—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 diseases not provided for elsewhere
-
- 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
- Y10S530/843—Digestive system
- Y10S530/845—Pancreas
-
- 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
- Y10S530/866—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof involving immunoglobulin or antibody fragment, e.g. fab', fab, fv, fc, heavy chain or light chain
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Hematology (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Diabetes (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Animal Behavior & Ethology (AREA)
- Emergency Medicine (AREA)
- Endocrinology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Obesity (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Gastroenterology & Hepatology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Hospice & Palliative Care (AREA)
- Oncology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (14)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE8604270A SE454299B (sv) | 1986-10-08 | 1986-10-08 | Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptiden |
| DE3751316T DE3751316T2 (de) | 1986-10-08 | 1987-10-07 | Materialzusammensetzung, welche ein Polypeptid aus Pankreas-Insel-Amyloid und/oder Antikörpern gegen dieses Polypeptid enthält, und Anwendung dieser Zusammensetzung. |
| AT87850300T ATE123147T1 (de) | 1986-10-08 | 1987-10-07 | Materialzusammensetzung, welche ein polypeptid aus pankreas-insel-amyloid und/oder antikörpern gegen dieses polypeptid enthält, und anwendung dieser zusammensetzung. |
| AU81012/87A AU8101287A (en) | 1986-10-08 | 1987-10-07 | Kit of material containing a polypeptide of pancreatic islet amyloid and/or antibodies directed against said polypeptide; and use of said kit of material |
| CA000548777A CA1341222C (en) | 1986-10-08 | 1987-10-07 | Preparations of islet amyloid polypeptide (iapp) and antibodies to iapp |
| EP87850300A EP0263802B1 (en) | 1986-10-08 | 1987-10-07 | Kit of material containing a polypeptide of pancreatic islet amyloid and/or antibodies directed against said polypeptide, and use of said kit of material |
| PCT/SE1987/000452 WO1988002863A1 (en) | 1986-10-08 | 1987-10-07 | Kit of material containing a polypeptide of pancreatic islet amyloid and/or antibodies directed against said polypeptide; and use of said kit of material |
| JP62506094A JP2863527B2 (ja) | 1986-10-08 | 1987-10-07 | 膵島アミロイドポリペプチド |
| ES87850300T ES2072252T3 (es) | 1986-10-08 | 1987-10-07 | Estuche de material que contiene un polipeptido de amiloide de los islotes y/o anticuerpos dirigidos contra dicho polipeptido, y uso de dicho estuche de material. |
| US07/516,329 US5116948A (en) | 1986-10-08 | 1990-04-30 | Preparations of islet amyloid polypeptide (iapp) and antibodies to iapp |
| US07/658,442 US5112945A (en) | 1986-10-08 | 1991-02-21 | Preparation of islet amyloid polypeptides (iapp) and antibodies to iapp |
| US07/838,043 US5298605A (en) | 1986-10-08 | 1992-02-19 | Antibodies to islet amyloid polypeptide (IAPP) and subunits thereof |
| US08/183,150 US5424221A (en) | 1986-10-08 | 1994-01-18 | Kit for detection of islet amyloid polypeptide (IAPP) |
| JP8199912A JP2939439B2 (ja) | 1986-10-08 | 1996-07-30 | 膵島アミロイドポリペプチドに対する抗体 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE8604270A SE454299B (sv) | 1986-10-08 | 1986-10-08 | Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptiden |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SE8604270D0 SE8604270D0 (sv) | 1986-10-08 |
| SE454299B true SE454299B (sv) | 1988-04-18 |
Family
ID=20365860
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SE8604270A SE454299B (sv) | 1986-10-08 | 1986-10-08 | Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptiden |
Country Status (10)
| Country | Link |
|---|---|
| US (2) | US5116948A (es) |
| EP (1) | EP0263802B1 (es) |
| JP (2) | JP2863527B2 (es) |
| AT (1) | ATE123147T1 (es) |
| AU (1) | AU8101287A (es) |
| CA (1) | CA1341222C (es) |
| DE (1) | DE3751316T2 (es) |
| ES (1) | ES2072252T3 (es) |
| SE (1) | SE454299B (es) |
| WO (1) | WO1988002863A1 (es) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5298605A (en) * | 1986-10-08 | 1994-03-29 | Regents Of The University Of Minnesota | Antibodies to islet amyloid polypeptide (IAPP) and subunits thereof |
| US5367052A (en) * | 1987-04-27 | 1994-11-22 | Amylin Pharmaceuticals, Inc. | Amylin peptides |
| GB8720115D0 (en) * | 1987-08-26 | 1987-09-30 | Cooper G J S | Treatment of diabetes mellitus |
| GB8709871D0 (en) * | 1987-04-27 | 1987-06-03 | Turner R C | Peptides |
| US5266561A (en) * | 1988-01-11 | 1993-11-30 | Amylin Pharmaceuticals, Inc. | Treatment of type 2 diabetes mellitus |
| US5175145A (en) * | 1988-08-26 | 1992-12-29 | Amylin Pharmaceuticals, Inc. | Treatment of diabetes mellitus with amylin agonists |
| HU222249B1 (hu) * | 1991-03-08 | 2003-05-28 | Amylin Pharmaceuticals Inc. | Eljárás amilin agonista peptidszármazékok és ezeket tartalmazó gyógyszerkészítmények előállítására |
| US5352771A (en) * | 1992-08-31 | 1994-10-04 | Iowa State University Research Foundation Inc. | Hydrolysis of peptide bonds using Pt (II) and Pd (II) complexes |
| US5376638A (en) * | 1992-09-01 | 1994-12-27 | Amylin Pharmaceuticals, Inc. | Methods for treating renin-related disorders with amylin antagonists |
| AU2992295A (en) * | 1994-07-13 | 1996-02-16 | Auckland Uniservices Limited | Therapeutic method and compounds of use therein |
| US6087129A (en) | 1996-01-19 | 2000-07-11 | Betagene, Inc. | Recombinant expression of proteins from secretory cell lines |
| US6821954B2 (en) | 1997-09-18 | 2004-11-23 | Auckland Uniservices Limited | Compounds and uses thereof in treating bone disorders |
| US6562836B1 (en) * | 1999-05-24 | 2003-05-13 | Queen's University Of Kingston | Methods and compounds for inhibiting amyloid deposits |
| EP1774339A2 (en) * | 2004-07-28 | 2007-04-18 | F. Hoffmann-Roche AG | Pancreatic polypeptide as target/marker of beta cell failure |
| DE102004051014A1 (de) * | 2004-10-20 | 2006-04-27 | Rwth Aachen | Chemisch modifizierte Peptidanaloga |
| CN118955675A (zh) * | 2019-02-22 | 2024-11-15 | 洛约拉马利蒙特大学 | Iapp肽、包含其的药物组合物及其应用 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE500044C2 (sv) * | 1985-02-15 | 1994-03-28 | Gambro Lundia Ab | Peptidförening, antiserum framställt med användning av denna förening samt användning av föreningen |
| GB8516081D0 (en) * | 1985-06-25 | 1985-07-31 | Ciba Geigy Ag | Assay & purification of amyloid components |
| GB8709871D0 (en) * | 1987-04-27 | 1987-06-03 | Turner R C | Peptides |
-
1986
- 1986-10-08 SE SE8604270A patent/SE454299B/sv not_active IP Right Cessation
-
1987
- 1987-10-07 WO PCT/SE1987/000452 patent/WO1988002863A1/en not_active Ceased
- 1987-10-07 CA CA000548777A patent/CA1341222C/en not_active Expired - Lifetime
- 1987-10-07 DE DE3751316T patent/DE3751316T2/de not_active Expired - Lifetime
- 1987-10-07 AT AT87850300T patent/ATE123147T1/de not_active IP Right Cessation
- 1987-10-07 ES ES87850300T patent/ES2072252T3/es not_active Expired - Lifetime
- 1987-10-07 AU AU81012/87A patent/AU8101287A/en not_active Abandoned
- 1987-10-07 EP EP87850300A patent/EP0263802B1/en not_active Expired - Lifetime
- 1987-10-07 JP JP62506094A patent/JP2863527B2/ja not_active Expired - Lifetime
-
1990
- 1990-04-30 US US07/516,329 patent/US5116948A/en not_active Expired - Lifetime
-
1991
- 1991-02-21 US US07/658,442 patent/US5112945A/en not_active Expired - Lifetime
-
1996
- 1996-07-30 JP JP8199912A patent/JP2939439B2/ja not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| DE3751316D1 (de) | 1995-06-29 |
| US5116948A (en) | 1992-05-26 |
| JP2939439B2 (ja) | 1999-08-25 |
| AU8101287A (en) | 1988-05-06 |
| EP0263802B1 (en) | 1995-05-24 |
| EP0263802A1 (en) | 1988-04-13 |
| WO1988002863A1 (en) | 1988-04-21 |
| US5112945A (en) | 1992-05-12 |
| ATE123147T1 (de) | 1995-06-15 |
| JPH02500857A (ja) | 1990-03-22 |
| JPH09119929A (ja) | 1997-05-06 |
| CA1341222C (en) | 2001-05-01 |
| DE3751316T2 (de) | 1996-02-01 |
| SE8604270D0 (sv) | 1986-10-08 |
| JP2863527B2 (ja) | 1999-03-03 |
| ES2072252T3 (es) | 1995-07-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Westermark et al. | Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. | |
| SE454299B (sv) | Sats innehallande polypeptid som finns i pankreasoamyloid och/eller antikroppar riktade mot polypeptiden | |
| Altstein et al. | An immunochemical analysis of oxytocin and vasopressin prohormone processing in vivo | |
| CN103298836B (zh) | 用于获得抗疏水性肽抗体的抗原的制备方法 | |
| US6638771B1 (en) | Composition and method for diagnosing auto-immune hepatitis | |
| Graindorge et al. | Radioimmunologic method for detection of antitubular basement membrane antibodies | |
| US5424221A (en) | Kit for detection of islet amyloid polypeptide (IAPP) | |
| CN105137071A (zh) | 心肌肌钙蛋白i均相酶免疫法测定试剂盒 | |
| Barnard et al. | Immunological studies with human aortic elastin | |
| JPH083486B2 (ja) | 体液中の基底膜コラーゲンの測定法及び基底膜コラーゲン―ドメインｎｃ１に対する抗体の検出法 | |
| CN101466732A (zh) | Iv型胶原样免疫反应性多肽 | |
| Leung et al. | Colonic tumor membrane-associated glycoprotein: Isolation of antigenically-active peptides after chemical cleavage | |
| KR100742115B1 (ko) | 조피볼락의 다클론 항체를 이용한 성숙도 판정방법 | |
| Costopoulou et al. | Direct ELISA method for the specific determination of prothymosin alpha in human specimens | |
| Tai et al. | Comparison of the major proteins of shark myelin with the proteins of higher vertebrates | |
| Cocchiara et al. | Purification of Par j I, a major allergen from Parietaria judaica pollen | |
| Leroy | Precipitating and complement-fixing antibodies to collagen with species and collagen subunit specificity | |
| US5516643A (en) | Immunochemical assays for cancer-associated SCM-recognition factor | |
| Lüning et al. | Amino acid sequence identity of TPA fragments from different sources | |
| JPH09178742A (ja) | 肺小細胞癌検出薬及びその使用 | |
| JP5354158B2 (ja) | 抗デカン酸修飾型グレリン抗体、デカン酸修飾型グレリン測定方法、およびデカン酸修飾型グレリン分離回収方法 | |
| CN115043927A (zh) | 针对抗α-突触核蛋白K80Hcy抗体的抗原肽及其应用 | |
| SE459372B (sv) | Humant pankreasspecifikt protein (hpasp), framstaellning av antikroppar mot proteinet och diagnostiskt foerfarande vid akut pankreatit | |
| Rogol | CYANOGEN BROMIDE FRAGMENTS AND PARTIAL AMINO ACID SEQUENCE OF BOVINE GROWTH HORMONE | |
| VidaliS | Availability of Hyperacetylated H4 Histone in Intact Nucleosomes to Specific Antibodies |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| NAL | Patent in force |
Ref document number: 8604270-2 Format of ref document f/p: F |
|
| NUG | Patent has lapsed |