ISOLATION AND PROPERTIES OF CASEIN KINASES FROM HUMAN PLATELETS
ISOLATION AND PROPERTIES OF CASEIN KINASES FROM HUMAN PLATELETS
复制标题
人血小板酪蛋白激酶的分离和性质
DOI:
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发表时间:
1982
期刊:
影响因子:
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通讯作者:
H. Yamamura
中科院分区:
文献类型:
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作者:
Akira Kikuchi;S. Tomisaka;K. Yonezawa;A. Sano;H. Yamamura
Two cyclic AMP-independent casein kinases were partially purified from human platelets by chromatography on DEAE-sephacel and phosphocellulose, and desig-nated CK-I and CK-II. These kinases differ as follows: 1) the molecular weight of CK-I is about 48,000 and that of CK-II is about 130,000; 2) optimum pH and Mg“, Km for ATP and casein are similar but not identical in these enzymes; 3) heparin can inhibit CK-II completely, but it cannot inhibit CK-I; 4) polylysine stimulates CK-II, but it cannot stimulate CK-I; 5) NaCl (200 mM) stimulates the activity of CK-II about 400 %, but CK-I is stimulated by NaCl only 20%; 6) although CK-I can phosphorylate only seryl residue of casein, CK-II can phosphorylate both seryl and threonyl residue in about equal amounts. These results show that CK-I and CK-II have quite different physical and kinetic properties, and the physiological role of these kinases in human platelets seems to be different.
DOI:
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发表时间:
1980
期刊:
The Journal of biological chemistry
影响因子:
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作者:
Hathaway,GM;Lubben,TH;Traugh,JA
通讯作者:
Traugh,JA