Autor: |
J H Robinson, C. Entwisle, G.M.P. Lawrence, C.G. Chapman, A.W.R. Tyrrell, M.J. Browne, B. Reavy, Ian B. Dodd, A.F. Esmail, J.E. Carey |
Rok vydání: |
1988 |
Předmět: |
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Zdroj: |
Journal of Biological Chemistry. 263:1599-1602 |
ISSN: |
0021-9258 |
DOI: |
10.1016/s0021-9258(19)77918-6 |
Popis: |
The complete cDNA for human tissue-type plasminogen activator (t-PA) was cloned and sequenced. A mutant was constructed by using in vitro site-specific mutagenesis to delete the region encoding the growth factor domain (amino acids 51-87 inclusive). Normal and mutant t-PA species were produced using two mammalian expression systems (in human HeLa cells and mouse C127 cells). The clearance of mutant and normal t-PA from plasma was examined in vivo using a guinea pig model. Mutant t-PA derived from HeLa or C127 cells was cleared much more slowly than the cognate normal t-PA. The potential role of the growth factor domain in the recognition of t-PA by the hepatic clearance mechanism is discussed. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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