Abstract:
:The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and KM = 310 X 10(-6) M. Comparison of these values with those determined previously for native fibrinogen and for a series of similar synthetic peptides, together with information about the amino acid sequences of this portion of the A alpha chain of abnormal fibrinogens, suggests an important role for Asp at position P10. Differences in the Michaelis-Menten parameters between F-8 and the 51-residue N-terminal CNBr fragment of the A alpha chain of fibrinogen correspond to only 1-2 kcal/mol in binding affinity.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Marsh HC Jr,Meinwald YC,Thannhauser TW,Scheraga HAdoi
10.1021/bi00287a002subject
Has Abstractpub_date
1983-08-30 00:00:00pages
4170-4issue
18eissn
0006-2960issn
1520-4995journal_volume
22pub_type
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