Structure and function of two novel serum proteinase inhibitors
| Project/Area Number |
60580142
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Kinki University |
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Principal Investigator |
SINOHARA Hyogo Kinki University School of Medicine, 医学部, 教授 (60088515)
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| Co-Investigator(Kenkyū-buntansha) |
SAITO Akio Kinki University School of Medicine, 医学部, 講師 (40153788)
SUZUKI Yasuyuki Kinki University School of Medicine, 医学部, 講師 (20019673)
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| Project Period (FY) |
1985 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1987: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1986: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1985: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | 血清プロテアーゼインヒビター / ムリノグロブリン / α_1-アンチトリプシン / コントラプシン / α_2-マクログロブリン / 血漿プロチアーゼインヒビター / α-1-アンチキモトリプシン |
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| Research Abstract |
Tow novel proteinase inhibitors,tentatively termed contarpsin and murino-globulin,were purified to homogeneity to homogeneity from fat, mouse and guinea pig,and their cemical,physicochemical and proteinase-inhibiting properties were compared with each other and with other known plasma proteinase inhibitors. Rodent contrapsin was found to be homologous with human algha-1-antichymotrypsin,but their inhibitory spectrum differed strikingly. Contrapsin was active against trypsin-like proteinases but not against chymotrypsin-like proteinases,whereas the reverse was true for alpha-1-antichymotrypsin. This difference was due to a marked change in the reactive site region the evolution. Only one amino acid was shared over the stretch of 10 amino acids encompassing the reactive ceter.
No plasma protein correspoinding to rodent murinoglobulin was detected in humans of rabbits. However, human or rabbit contained a protein having the trypsin-protein amidase activity. This protein was identified as alpha-1-antitrypsin. This indicates that under certain conditions, alpha-1-anti-trypsin interacts with trypsin in such a manner that the active aite of trypsin remains unattacked while the access of large substrate to it is prevented. Such interaction has not been reported.
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Report
(2 results)
Research Products
(14 results)
