Abstract:
:Zinc cations at concentrations of 0.2 mM and greater catalyzed specific phosphorylation, by ATP, of two membrane-associated proteins from rat hippocampus. These proteins, corresponding to molecular weights of 60 and 49 kDa, were phosphorylated primarily at tyrosine residues. The 60-kDa protein was identified as p60c-src by immunoprecipitation using two different p60src-specific monoclonal antibodies. The 49-kDa protein co-immunoprecipitated with p60c-src. Cyanogen bromide cleavage of p60c-src and the 49-kDa protein phosphorylated in the presence of Zn2+ gave different patterns of phosphopeptides. It is suggested that tyrosine phosphorylation of p60c-src and the p60c-src-associated 49-kDa protein may be a way of zinc participation in hippocampal neurotransmission.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vener AV,Loeb Jdoi
10.1016/0014-5793(92)80534-nkeywords:
subject
Has Abstractpub_date
1992-06-01 00:00:00pages
261-4issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(92)80534-Njournal_volume
303pub_type
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