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Comparison of tyrosine phosphorylation of proteins by membrane fractions from mouse liver, ehrlich ascites tumor and MH134 hepatoma
Author(s) -
Usui Hirofumi,
Yoshikawa Kazunori,
Imazu Michinori,
Tsukamoto Haruhisa,
Takeda Masao
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80653-0
Subject(s) - membrane , phosphorylation , tyrosine , biochemistry , ascites , membrane protein , polyacrylamide gel electrophoresis , gel electrophoresis , biology , chemistry , microbiology and biotechnology , enzyme , medicine
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 NaV0 3 , 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.