JP2657053C - - Google Patents
Info
- Publication number
- JP2657053C JP2657053C JP2657053C JP 2657053 C JP2657053 C JP 2657053C JP 2657053 C JP2657053 C JP 2657053C
- Authority
- JP
- Japan
- Prior art keywords
- pthrp
- amino acid
- fragment
- human pthrp
- acid sequence
- 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 - Lifetime
Links
- 108010090228 Parathyroid Hormone-Related Protein Proteins 0.000 claims description 163
- 102000012961 Parathyroid Hormone-Related Protein Human genes 0.000 claims description 163
- 230000000694 effects Effects 0.000 claims description 62
- 108090001123 antibodies Proteins 0.000 claims description 45
- 102000004965 antibodies Human genes 0.000 claims description 45
- 150000001413 amino acids Chemical class 0.000 claims description 34
- 238000004166 bioassay Methods 0.000 claims description 25
- 102000004169 proteins and genes Human genes 0.000 claims description 24
- 108090000623 proteins and genes Proteins 0.000 claims description 24
- 241000283690 Bos taurus Species 0.000 claims description 17
- 239000003153 chemical reaction reagent Substances 0.000 claims description 17
- 230000004044 response Effects 0.000 claims description 13
- 102000003982 Parathyroid hormone Human genes 0.000 claims description 12
- 108090000445 Parathyroid hormone Proteins 0.000 claims description 12
- 239000000199 parathyroid hormone Substances 0.000 claims description 12
- 229960001319 parathyroid hormone Drugs 0.000 claims description 12
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 12
- 108060000200 EC 4.6.1.1 Proteins 0.000 claims description 11
- 102000019460 EC 4.6.1.1 Human genes 0.000 claims description 11
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 10
- 230000000875 corresponding Effects 0.000 claims description 10
- 230000001809 detectable Effects 0.000 claims description 8
- 239000011159 matrix material Substances 0.000 claims description 7
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 5
- 230000002163 immunogen Effects 0.000 claims description 4
- 238000010790 dilution Methods 0.000 claims description 3
- UIIMBOGNXHQVGW-UHFFFAOYSA-M buffer Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 claims description 2
- 229920001184 polypeptide Polymers 0.000 claims 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 210000004027 cells Anatomy 0.000 description 44
- 235000001014 amino acid Nutrition 0.000 description 27
- 235000018102 proteins Nutrition 0.000 description 22
- WEVYAHXRMPXWCK-UHFFFAOYSA-N acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 20
- 238000004519 manufacturing process Methods 0.000 description 18
- 241000700159 Rattus Species 0.000 description 16
- 238000004128 high performance liquid chromatography Methods 0.000 description 16
- 239000000499 gel Substances 0.000 description 15
- 201000008968 osteosarcoma Diseases 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 12
- 201000011510 cancer Diseases 0.000 description 12
- 238000000746 purification Methods 0.000 description 12
- 229940095074 Cyclic AMP Drugs 0.000 description 10
- IVOMOUWHDPKRLL-KQYNXXCUSA-N cAMP Chemical compound C([C@H]1O2)OP(O)(=O)O[C@H]1[C@@H](O)[C@@H]2N1C(N=CN=C2N)=C2N=C1 IVOMOUWHDPKRLL-KQYNXXCUSA-N 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 238000003127 radioimmunoassay Methods 0.000 description 9
- 239000000523 sample Substances 0.000 description 9
- 229940088597 Hormone Drugs 0.000 description 8
- 241000283973 Oryctolagus cuniculus Species 0.000 description 8
- 230000006399 behavior Effects 0.000 description 8
- 239000005556 hormone Substances 0.000 description 8
- 230000003211 malignant Effects 0.000 description 8
- 239000002609 media Substances 0.000 description 8
- 238000004007 reversed phase HPLC Methods 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- DTQVDTLACAAQTR-UHFFFAOYSA-N trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 8
- UDMBCSSLTHHNCD-KQYNXXCUSA-N Adenosine monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 description 7
- 229950006790 Adenosine phosphate Drugs 0.000 description 7
- 239000000969 carrier Substances 0.000 description 7
- 238000010828 elution Methods 0.000 description 7
- 108010054971 parathyroid hormone-related protein (1-34) Proteins 0.000 description 7
- 239000012071 phase Substances 0.000 description 7
- XUJNEKJLAYXESH-REOHCLBHSA-N L-cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 6
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 150000003180 prostaglandins Chemical class 0.000 description 6
- 108090000745 Immune Sera Proteins 0.000 description 5
- 210000002826 Placenta Anatomy 0.000 description 5
- 229940082622 Prostaglandin cardiac therapy preparations Drugs 0.000 description 5
- 229940077717 Prostaglandin drugs for peptic ulcer and gastro-oesophageal reflux disease (GORD) Drugs 0.000 description 5
- 229920005654 Sephadex Polymers 0.000 description 5
- 239000012507 Sephadex™ Substances 0.000 description 5
- 210000002966 Serum Anatomy 0.000 description 5
- 108010049264 Teriparatide Proteins 0.000 description 5
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 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 5
- 238000004113 cell culture Methods 0.000 description 5
- 229940094443 oxytocics Prostaglandins Drugs 0.000 description 5
- 229960001322 trypsin Drugs 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 206010020583 Hypercalcaemia Diseases 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 230000003042 antagnostic Effects 0.000 description 4
- 230000000975 bioactive Effects 0.000 description 4
- 239000003636 conditioned culture media Substances 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 230000000148 hypercalcaemia Effects 0.000 description 4
- 210000000963 osteoblast Anatomy 0.000 description 4
- 230000000790 osteoblast Effects 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 210000001519 tissues Anatomy 0.000 description 4
- 210000004369 Blood Anatomy 0.000 description 3
- 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 3
- 102000004414 Calcitonin gene-related peptide Human genes 0.000 description 3
- 108090000932 Calcitonin gene-related peptide Proteins 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- 108020004999 Messenger RNA Proteins 0.000 description 3
- 206010028980 Neoplasm Diseases 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 229920000272 Oligonucleotide Polymers 0.000 description 3
- 241000283898 Ovis Species 0.000 description 3
- 101710027813 PTRH1 Proteins 0.000 description 3
- 210000002990 Parathyroid Glands Anatomy 0.000 description 3
- 108010033276 Peptide Fragments Proteins 0.000 description 3
- 102000007079 Peptide Fragments Human genes 0.000 description 3
- 102000001938 Plasminogen Activators Human genes 0.000 description 3
- 108010001014 Plasminogen Activators Proteins 0.000 description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 239000005557 antagonist Substances 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 230000001419 dependent Effects 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 229920002106 messenger RNA Polymers 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 101710006356 ACTI Proteins 0.000 description 2
- 208000006386 Bone Resorption Diseases 0.000 description 2
- 210000000988 Bone and Bones Anatomy 0.000 description 2
- 101700046715 CSTI Proteins 0.000 description 2
- 108060001064 Calcitonin Proteins 0.000 description 2
- 102400000113 Calcitonin Human genes 0.000 description 2
- 229960004015 Calcitonin Drugs 0.000 description 2
- 102000008130 Cyclic AMP-Dependent Protein Kinases Human genes 0.000 description 2
- 108010049894 Cyclic AMP-Dependent Protein Kinases Proteins 0.000 description 2
- 101700020566 DEFA4 Proteins 0.000 description 2
- KAQKFAOMNZTLHT-VVUHWYTRSA-N Epoprostenol Chemical compound O1C(=CCCCC(O)=O)C[C@@H]2[C@@H](/C=C/[C@@H](O)CCCCC)[C@H](O)C[C@@H]21 KAQKFAOMNZTLHT-VVUHWYTRSA-N 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 240000007842 Glycine max Species 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 101710006353 IP3R Proteins 0.000 description 2
- 101700035656 ISOTI Proteins 0.000 description 2
- 101700035039 ITI Proteins 0.000 description 2
- 101700052013 ITR2 Proteins 0.000 description 2
- 101700068039 ITRP Proteins 0.000 description 2
- 108010044467 Isoenzymes Proteins 0.000 description 2
- 210000003734 Kidney Anatomy 0.000 description 2
- 210000000265 Leukocytes Anatomy 0.000 description 2
- 101700036939 MTI Proteins 0.000 description 2
- 230000036740 Metabolism Effects 0.000 description 2
- -1 Olesein Chemical compound 0.000 description 2
- 101000032483 PTH Proteins 0.000 description 2
- 102000001253 Protein Kinases Human genes 0.000 description 2
- 108060006633 Protein Kinases Proteins 0.000 description 2
- 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 2
- 101700062451 TI Proteins 0.000 description 2
- 108010046334 Urease Proteins 0.000 description 2
- 210000002700 Urine Anatomy 0.000 description 2
- 150000001408 amides Chemical class 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000024279 bone resorption Effects 0.000 description 2
- 229960003773 calcitonin (salmon synthetic) Drugs 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000003729 cation exchange resin Substances 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000010192 crystallographic characterization Methods 0.000 description 2
- 229920003013 deoxyribonucleic acid Polymers 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 229960001123 epoprostenol Drugs 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 230000003054 hormonal Effects 0.000 description 2
- 102000036364 human PTH protein Human genes 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 230000035786 metabolism Effects 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000006011 modification reaction Methods 0.000 description 2
- 108010045030 monoclonal antibodies Proteins 0.000 description 2
- 230000000849 parathyroid Effects 0.000 description 2
- 230000036961 partial Effects 0.000 description 2
- 108060006184 phycobiliprotein family Proteins 0.000 description 2
- 229920000915 polyvinyl chloride Polymers 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 229940120657 salmon calcitonin Drugs 0.000 description 2
- 108010068072 salmon calcitonin Proteins 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 230000004936 stimulating Effects 0.000 description 2
- 239000002753 trypsin inhibitor Substances 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- APIXJSLKIYYUKG-UHFFFAOYSA-N 3-Isobutyl-1-methyl-2,6(1H,3H)-purinedione Chemical compound O=C1N(C)C(=O)N(CC(C)C)C2=C1N=CN2 APIXJSLKIYYUKG-UHFFFAOYSA-N 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N AI2O3 Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- 101710027066 ALB Proteins 0.000 description 1
- 208000003200 Adenoma Diseases 0.000 description 1
- 206010001233 Adenoma benign Diseases 0.000 description 1
- 241000288007 Alectoris chukar Species 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 101710027538 Aper1 Proteins 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 208000003432 Bone Disease Diseases 0.000 description 1
- 229940098773 Bovine Serum Albumin Drugs 0.000 description 1
- 108091003117 Bovine Serum Albumin Proteins 0.000 description 1
- IXIBAKNTJSCKJM-BUBXBXGNSA-N Bovine insulin 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)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)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(C)C)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 IXIBAKNTJSCKJM-BUBXBXGNSA-N 0.000 description 1
- 210000000621 Bronchi Anatomy 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 210000000170 Cell Membrane Anatomy 0.000 description 1
- 208000009863 Chronic Kidney Failure Diseases 0.000 description 1
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 1
- 102400000739 Corticotropin Human genes 0.000 description 1
- 101800000414 Corticotropin Proteins 0.000 description 1
- ZOOGRGPOEVQQDX-UUOKFMHZSA-N Cyclic guanosine monophosphate Chemical compound C([C@H]1O2)OP(O)(=O)O[C@H]1[C@@H](O)[C@@H]2N1C(N=C(NC2=O)N)=C2N=C1 ZOOGRGPOEVQQDX-UUOKFMHZSA-N 0.000 description 1
- 102000033147 ERVK-25 Human genes 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 230000036826 Excretion Effects 0.000 description 1
- 230000035693 Fab Effects 0.000 description 1
- 102000008857 Ferritin Human genes 0.000 description 1
- 108050000784 Ferritin Proteins 0.000 description 1
- 238000008416 Ferritin Methods 0.000 description 1
- 210000003754 Fetus Anatomy 0.000 description 1
- HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 108060001084 Luciferase family Proteins 0.000 description 1
- 210000004072 Lung Anatomy 0.000 description 1
- 229920002521 Macromolecule Polymers 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 206010033964 Parathyroid tumour benign Diseases 0.000 description 1
- 108091005771 Peptidases Proteins 0.000 description 1
- 240000004713 Pisum sativum Species 0.000 description 1
- 235000010582 Pisum sativum Nutrition 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- XBDQKXXYIPTUBI-UHFFFAOYSA-N Propionic acid Substances CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010038444 Renal failure chronic Diseases 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N Rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 240000003670 Sesamum indicum Species 0.000 description 1
- 235000003434 Sesamum indicum Nutrition 0.000 description 1
- 206010041823 Squamous cell carcinoma Diseases 0.000 description 1
- RZWIIPASKMUIAC-VQTJNVASSA-N Thromboxane Chemical compound CCCCCCCC[C@H]1OCCC[C@@H]1CCCCCCC RZWIIPASKMUIAC-VQTJNVASSA-N 0.000 description 1
- 235000015450 Tilia cordata Nutrition 0.000 description 1
- 235000011941 Tilia x europaea Nutrition 0.000 description 1
- 102000009618 Transforming Growth Factors Human genes 0.000 description 1
- 108010009583 Transforming Growth Factors Proteins 0.000 description 1
- 230000036462 Unbound Effects 0.000 description 1
- 101700071818 VGK Proteins 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000000240 adjuvant Effects 0.000 description 1
- 230000003466 anti-cipated Effects 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 230000000890 antigenic Effects 0.000 description 1
- 108091007172 antigens Proteins 0.000 description 1
- 102000038129 antigens Human genes 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000037348 biosynthesis Effects 0.000 description 1
- 210000002449 bone cell Anatomy 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 239000006143 cell culture media Substances 0.000 description 1
- 230000001413 cellular Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000001054 cortical Effects 0.000 description 1
- IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 1
- 229960000258 corticotropin Drugs 0.000 description 1
- 210000004748 cultured cells Anatomy 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000003436 cytoskeletal Effects 0.000 description 1
- 230000004059 degradation Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drugs Drugs 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000001605 fetal Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000002068 genetic Effects 0.000 description 1
- 230000000121 hypercalcemic Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002055 immunohistochemical Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular Effects 0.000 description 1
- 238000009114 investigational therapy Methods 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000004571 lime Substances 0.000 description 1
- 230000000670 limiting Effects 0.000 description 1
- 230000002503 metabolic Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000000051 modifying Effects 0.000 description 1
- 102000005614 monoclonal antibodies Human genes 0.000 description 1
- 230000000877 morphologic Effects 0.000 description 1
- 230000001264 neutralization Effects 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 230000001582 osteoblastic Effects 0.000 description 1
- 201000003686 parathyroid adenoma Diseases 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 238000000819 phase cycle Methods 0.000 description 1
- 239000002571 phosphodiesterase inhibitor Substances 0.000 description 1
- 230000037081 physical activity Effects 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920001467 poly(styrenesulfonates) Polymers 0.000 description 1
- 108091008117 polyclonal antibodies Proteins 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000002089 prostaglandin antagonist Substances 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive Effects 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000002829 reduced Effects 0.000 description 1
- 239000003488 releasing hormone Substances 0.000 description 1
- 230000000268 renotropic Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 108091007521 restriction endonucleases Proteins 0.000 description 1
- 229910052702 rhenium Inorganic materials 0.000 description 1
- 238000002390 rotary evaporation Methods 0.000 description 1
- 230000001568 sexual Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 201000010874 syndrome Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing Effects 0.000 description 1
- 239000005495 thyroid hormone Substances 0.000 description 1
- 239000000700 tracer Substances 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 210000004881 tumor cells Anatomy 0.000 description 1
- 239000011710 vitamin D Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- WQZGKKKJIJFFOK-FPRJBGLDSA-N β-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 1
Family
ID=
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2657053B2 (ja) | ＰＴＨｒＰ又はその断片に対する抗体及びこの抗体を含むキット | |
| Niall et al. | The chemistry of growth hormone and the lactogenic hormones | |
| KRAMER et al. | Immunological identification and distribution of parathyroid hormone-like protein polypeptides in normal and malignant tissues | |
| US7799533B2 (en) | Polypeptides, their production and use | |
| US5217896A (en) | Monoclonal antibodies recognizing parathyroid hormone-like protein | |
| Martin et al. | Parathyroid hormone-related protein: isolation, molecular cloning, and mechanism of action | |
| JP4374316B2 (ja) | β−アミロイドまたはその誘導体に対する抗体およびその用途 | |
| Zajac et al. | Biosynthesis of calcitonin by human lung cancer cells | |
| MACISAAC et al. | Ontogeny of parathyroid hormone-related protein in the ovine parathyroid gland | |
| STEWART et al. | Synthetic parathyroid hormone-like protein-(1–74): Biochemical and physiological characterization | |
| Dickinson et al. | Expression and processing of prohormones in nonendocrine cells | |
| JP2657053C (fi) | ||
| Yanaihara et al. | Application of region-specific immunoassay for human chromogranin A: substantial clue for detection and measurement of chromogranin A in human plasma | |
| JP2648952B2 (ja) | 種々の病理的状態に於いてｐｓ２遺伝子から特異的に発現される蛋白質及びその断片、該蛋白質及び／又はその断片から得られる抗体、並びに病理的状態に対する検出、診断及び治療への該蛋白質、その断片及び抗体の適用 | |
| AU598561B2 (en) | A protein active in humoral hypercalcemia of malignancy-pthrp | |
| JP2598801C (fi) | ||
| Wildey et al. | Phosphorylation state of pro-atrial natriuretic factor in rat atrial secretory granules | |
| JP3025002B2 (ja) | Ｄｎａ、ポリペプチド、抗体、およびそれらの用途 | |
| JP4306865B2 (ja) | 新規生理活性ペプチドおよびその用途 | |
| JPH04218388A (ja) | ソマトトロピン結合蛋白質を特異的に認識する抗体 | |
| JP2980991B2 (ja) | 癌遺伝子Ｋ−ｓａｍの遺伝子産物に対する抗体、その用途およびペプチド | |
| JPH0570482A (ja) | ペプチドおよびその塩 | |
| Akamizu et al. | Thyrotropin Receptor | |
| JPH07508341A (ja) | 生物サンプルおよび体液中の正常細胞と悪性腫瘍細胞とにおける分化マーカーの検出方法 | |
| US20050202439A1 (en) | Epididymis-specific receptor protein and its use |