Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P sub(10)

A fibrinogen peptide fragment was synthesized by classical methods in solution (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be k sub(cat) = 31 x 10 super(-11) M (NIH unit/L)s) super(-1) and K sub(M) = 310 x 10 super(-6 M. Compari...

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Bibliographic Details
Published in:Biochemistry (Easton) 1983-01, Vol.22 (18), p.4170-4174
Main Authors: Marsh, HC Jr, Meinwald, Y C, Thannhauser, T W, Scheraga, HA
Format: Article
Language:English
Subjects:
fibrinogen
peptide synthesis
thrombin
Online Access:Get full text
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Summary:A fibrinogen peptide fragment was synthesized by classical methods in solution (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be k sub(cat) = 31 x 10 super(-11) M (NIH unit/L)s) super(-1) and K sub(M) = 310 x 10 super(-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 P) sub(1)0 )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.
ISSN:0006-2960