The C-terminal binding domain of hirullin P18: Antithrombin activity and comparison to hirudin peptides
Hirullin P18 is a 61-amino acid hirudin-related protein having potent antithrombin activity. Similar to hirudin, it contains a highly acidic C-terminus, but has a significantly different sequence from any other known hirudin variant. The present study demonstrates that the C-terminal fragment acetyl...
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Published in | FEBS letters Vol. 269; no. 2; pp. 425 - 429 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
03.09.1990
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Hirullin P18 is a 61-amino acid hirudin-related protein having potent antithrombin activity. Similar to hirudin, it contains a highly acidic C-terminus, but has a significantly different sequence from any other known hirudin variant. The present study demonstrates that the C-terminal fragment acetyl-hirullin P18
40–61 possesses an antithrombin potency similar to that of acetyl-desulfatohirudin
45–65. Additionally, like the hirudin fragment analog, it inhibits fibrin-clot formation by binding to a non-catalytic site on thrombin. Sequential shortening of the hirullin P18 C-terminal fragment demonstrates the critical nature of Phe
51, which corresponds to the important Phe
56 residue of hirudin. Although the sequences of hirullin P18
54–61 and hirudin
59–65 have substantial differences, the C-terminal functional domain represented by hirullin P18
50–61 appears to be comparable to hirudin
55–65 in terms of its functional role in antithrombin activity. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(90)81208-6 |