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Platelet Ca2+-activated, phospholipid-dependent protein kinase: evidence for proteolytic activation of the enzyme in cells treated with phospholipase C1.

Authors
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Volume
118
Issue
3
Pages
835–841
Identifiers
PMID: 6231025
Source
Medline
License
Unknown

Abstract

Incubation of human platelets with C. perfringens phospholipase C caused an increase in soluble protein kinase activity assayed in the presence of EGTA, and a decrease in Ca2+/phospholipid-dependent protein kinase activity. Fractionation of extracts on DEAE-cellulose columns showed that phospholipase C treatment resulted in a new peak of protein kinase active in the presence of EGTA. On Sephadex G-100 chromatography this enzyme eluted as a single peak of protein kinase activity of MW about 50,000. An extract from untreated platelets eluted as a single peak of Ca2+/phospholipid-dependent protein kinase of MW about 77,000. It was concluded that phospholipase C treatment resulted in the proteolysis of this latter enzyme to the lower MW form.

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