Two separate tyrosine protein kinases in human platelets

FEBS Letters

Takeuchi, Fumito²  Nakamura, Shun-ichi²  Tomizawa, Tamami²  Takasaki, Noriko²  Yamamura, Hirohei²  Kondo, Hiroki¹ 

[1] Department of Industrial Chemistry, Faculty ofEngineering, Nagasaki University, Bunkyo, Nagasaki 825, Japan;Department of Biochemistry, Fukui Medical School, Matsuoka, Fukui 910-11 Nagasaki 825, Japan

关键词: Tyrosine protein kinase;    Human platelet;    Cytosomal enzyme;    Protein phosphorylation;    NP 40;    Nonidet P-40;    TLCK;    p-tosyl-L-lysine chloromethyl ketone;    TPCK;    p-tosyl-L-phenylalanine chloromethyl ketone;    PC-TPK;    platelet cytosolic tyrosine protein kinase;    PM-TPK;    platelet membrane-associated tyrosine protein kinase;    protein kinase C;    Ca2+-activated;    phospholipid-dependent protein kinase;   

DOI  :  10.1016/0014-5793(85)80652-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tyrosine protein kinase activities were detected in the cytosolic fraction (PC-TPK) and the particulate fraction (PM-TPK) in human platelets using the synthetic peptide, E₁₁G₁, (Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Arg-Gly) as a substrate. PC-TPK and PM-TPK were different in substrate specificities, divalent cation requirements and apparent M _r values. These results strongly suggest that in platelets there exist at least two separate tyrosine protein kinases; one is present in cytosol and the other might be associated with membranes.

【 授权许可】

Unknown