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Calcium effects on prothrombin and its reaction with bifunctional alkylating reagents.

Abstract：

:Monodisperse bovine prothrombin was prepared and its molecular states under several conditions examined. The protein showed no tendency to self-associate in the absence of calcium. Calcium (4 mM) caused small increases in the apparent molecular weight of the protein which may or may not represent protein dimerization with very low affinity. The allowed conclusion was that calcium-induced prothrombin dimerization is minimal up to protein concentrations of many mg/ml. Calcium-induced protein shape changes did not measurably alter the protein diffusion constant. A bifunctional alkylating reagent did produce extensive calcium-dependent prothrombin crosslinking. Prothrombin dimers formed by the crosslinking agent were not a measure of the state of native prothrombin.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Silversmith RE,Wei GJ,Nelsestuen GL

doi

10.1016/s0006-291x(83)80138-7

subject

Has Abstract

pub_date

1983-02-28 00:00:00

pages

213-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)80138-7

journal_volume

111

pub_type

杂志文章

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