Abstract:
:Human placental lipocortin is a high-affinity substrate for rat brain protein kinase C in vitro with phosphorylation occurring on serine and threonine residues in a ratio of approximately 2 to 1. Comparison of the ability of various N-terminal-truncated derivatives of lipocortin to serve as phosphorylation substrates, and direct analysis of the N-terminal peptides cleaved from 32P-labeled lipocortin, indicated that threonine-24, serine-27, and serine-28 were the phosphorylation sites. The possibility is discussed that a lysine residue near the carboxy side of the phosphorylation site was involved in lipocortin interaction with the catalytic site of protein kinase C.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Schlaepfer DD,Haigler HTdoi
10.1021/bi00412a008subject
Has Abstractpub_date
1988-06-14 00:00:00pages
4253-8issue
12eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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