A protein kinase system from platelet rich plasma.

Abstract:

:Treatment of platelet rich plasma (PRP) at pH 5 results in the precipitation of a protein kinase system. The protein kinase is associated with the platelet fraction and is capable of phosphorylation of several plasma proteins. Analysis of the 32P-labeled phosphoproteins by two dimensional gel electrophoresis showed the existence of three major phosphoproteins: 72K and 80K proteins with identical isoelectric points (pI) of 6.0 and another 72K protein with a pI of 6.8-7.0. This latter 72K phosphoprotein has recently been identified as the alpha-chain of fibrinogen. The identity of the other 2 proteins remains to be shown. The activity of the protein kinase is markedly enhanced by Mn2+, it phosphorylates calf thymus histone as an exogenous substrate and is independent of cAMP or cGMP. This protein kinase activity is inhibited competitively by ADP.

authors

Galabru J,Krust B,Hovanessian AG

doi

10.1016/0006-291x(83)91736-9

subject

Has Abstract

pub_date

1983-06-15 00:00:00

pages

370-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)91736-9

journal_volume

113

pub_type

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