ACTIVITY PHOSPHORYLATING TYROSINE IN POLYOMA T-ANTIGEN IMMUNOPRECIPITATES
ACTIVITY PHOSPHORYLATING TYROSINE IN POLYOMA T-ANTIGEN IMMUNOPRECIPITATES
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DOI：
10.1016/0092-8674(79)90205-8
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发表时间：
1979-01-01
期刊：
影响因子：
64.5
通讯作者：
HUNTER, T
中科院分区：
文献类型：
--
作者：
ECKHART, W;HUTCHINSON, MA;HUNTER, T
Polyoma T [tumor] antigen immunoprecipitates contain a protein kinase-like activity which preferentially phosphorylates material of 50-60,000 daltons MW. Phosphorylation is not diminished in extracts of polyoma tsA mutant-infected [mouse] cells shifted to the nonpermissive temperature late in infection, conditions which inactivate the large T antigen. Phosphorylation is reduced or absent in cells infected with polyoma host range nontransforming (hr-t) mutants, which have defective small and medium T antigens. The major acceptor of phosphate is not the H chain of immunoglobulin, but appears to be the polyoma medium T antigen. The large T antigen is also phosphorylated, but usually to a lower specific activity. In terms of acid and alkali sensitivity and electrophoretic and chromatographic mobility in 1 and 2 dimensions, the phosphorylated residue behaves identically to phosphotyrosine and differently than phosphorylated serine, threonine, lysine and histidine.
