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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1991-7-3
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pubmed:abstractText |
Limited tryptic proteolysis of homogeneous protein kinase C induces the formation of a catalytically active fragment of 50 kDa (kinase M) which, unlike native PK C acquires the ability to phosphorylate PIP. Both ATP and GTP were found to be capable of serving as phosphate donors in this process. Incubation of purified kinase M with a preparation of rat brain membrane fraction enhanced the level of phosphorylation of PIP in the presence and in the absence of exogenous PIP. A scheme of the interrelationship of phosphoinositide metabolism and the proteolytic processing of protein kinase C is proposed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1007-13
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1645534-Adenosine Triphosphate,
pubmed-meshheading:1645534-Animals,
pubmed-meshheading:1645534-Brain,
pubmed-meshheading:1645534-Kinetics,
pubmed-meshheading:1645534-Models, Biological,
pubmed-meshheading:1645534-Molecular Weight,
pubmed-meshheading:1645534-Peptide Fragments,
pubmed-meshheading:1645534-Phosphatidylinositol Phosphates,
pubmed-meshheading:1645534-Phosphatidylinositols,
pubmed-meshheading:1645534-Phosphorus Radioisotopes,
pubmed-meshheading:1645534-Phosphorylation,
pubmed-meshheading:1645534-Protein Kinase C,
pubmed-meshheading:1645534-Rats,
pubmed-meshheading:1645534-Rats, Inbred Strains,
pubmed-meshheading:1645534-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
Proteolytic fragment of protein kinase C (kinase M) phosphorylates in vitro phosphatidylinositol-4-phosphate.
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pubmed:affiliation |
M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR.
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pubmed:publicationType |
Journal Article
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