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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1985-10-17
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pubmed:abstractText |
Three peaks of tyrosine protein kinase activity (TK-I, TK-II and TK-III) can be resolved when the extract of rat spleen particulate fraction is subjected to DEAE-cellulose gradient chromatography. TK-I and TK-II, insensitive to both EGF and insulin, have been further purified by Sephacryl S200 gel filtration and characterized. TK-I has an apparent mR of 65000, by far prefers Mn2+ over Mg2+ as activator, can use GTP besides ATP as phosphate donor and is stimulated 2-3-fold by polylysine. TK-II, whose mR approximates 50000, is equally activated by Mg2+ and Mn2+, does not use GTP and is insensitive to polylysine. TK-I and TK-II can phosphorylate the synthetic peptide Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Arg-Gly (as well as its derivative with Orn in place of Arg), angiotensin II and poly(Glu, Tyr) 4:1 which exhibits different km values with TK-I and TK-II, (100 and 10 microM, respectively). When TK-I was incubated with [gamma-32P]ATP and MnCl2 a doublet of alkali-stable radiolabeled bands with molecular masses of 55 and 60 kDa were observed. Under identical conditions TK-II gives rise to a single alkali-stable radiolabeled band of 51 kDa, which may represent the autophosphorylation product of TK-II itself.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
188
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
321-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:4040873-Animals,
pubmed-meshheading:4040873-Chromatography, DEAE-Cellulose,
pubmed-meshheading:4040873-Chromatography, Gel,
pubmed-meshheading:4040873-Enzyme Activation,
pubmed-meshheading:4040873-Kinetics,
pubmed-meshheading:4040873-Protein Kinases,
pubmed-meshheading:4040873-Protein-Tyrosine Kinases,
pubmed-meshheading:4040873-Rats,
pubmed-meshheading:4040873-Spleen,
pubmed-meshheading:4040873-Substrate Specificity
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pubmed:year |
1985
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pubmed:articleTitle |
Isolation and partial characterization of distinct forms of tyrosine protein kinases from rat spleen.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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