Zn2+ enhances protein tyrosine kinase activity of human platelet membranes.

Abstract:

:In human platelet membranes enhanced tyrosine phosphorylation of certain proteins was observed when Zn2+ instead of Mg2+ or Mn2+ was used as a divalent cation for the kinase reaction. An enhanced level of phosphate incorporation into tyrosine residues occurred into a 68 kDa polypeptide besides the 45 kDa and 105 kDa proteins. Preincubation of platelet membranes with TBR-IgG showed a concentration-dependent inhibition of the phosphorylation of the 45, 68 and 105 kDa proteins. Moreover, pp60c-src, representing the major protein tyrosine kinase activity in platelets, was found to be stimulated by Zn2+. The data, thus, support the assumption that pp60c-src kinase is responsible for Zn2+ stimulated tyrosine phosphorylation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Findik D,Presek P

doi

10.1016/0014-5793(88)81232-8

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

51-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)81232-8

journal_volume

235

pub_type

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