Comparison of tyrosine phosphorylation of proteins by membrane fractions from mouse liver, ehrlich ascites tumor and MH134 hepatoma

FEBS Letters

Tsukamoto, Haruhisa¹  Takeda, Masao¹  Imazu, Michinori¹  Usui, Hirofumi¹  Yoshikawa, Kazunori¹ 

[1] Department of Biochemistry, Hiroshima University School of Medicine, Kasumi, Minami-ku, Hiroshima 734, Japan

关键词: Membrane protein;    Phosphorylation;    Phosphotyrosine;    EGF receptor;    Cancer;    EGF;    epidermal growth factor;    PMSF;    phenylmethylsulfonyl fluoride;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(85)80653-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

When membrane fractions from mouse liver. Ehrlich ascites tumor and MH 134 hepatoma were incubated with [γ-³²]ATP at O°C in the presence of MnCly ZnCl; and NaV0₃, proteins were phosphorylated on tyrosines to a larger extent in liver membranes than in tumor membranes. Separation of labelled proteins by SDS-gel electrophoresis showed phosphorylated alkali-resistant bands of 170, 140, 130, 80, 56, 53 and 46 kDa proteins in Ehrlich ascites tumor membranes; liver membranes exhibited more strongly phosphorylated bands of 170, 56, 53 and 46 kDa proteins. Epidermal growth factor stimulated the tyrosine phosphorylation of only a 170 kDa protein, which was more significant in liver membranes. Liver membranes exhibited slightly higher levels of tyrosine protein kinase activity compared to tumor membranes.

【 授权许可】

Unknown