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 Lettjournal_title
FEBS lettersauthors
Findik D,Presek Pdoi
10.1016/0014-5793(88)81232-8subject
Has Abstractpub_date
1988-08-01 00:00:00pages
51-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(88)81232-8journal_volume
235pub_type
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