Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin.
作者： V. Gerke , K. Weber
DOI: 10.1002/J.1460-2075.1984.TB01789.X
关键词:
摘要: Membrane vesicles derived from the apical side of procine intestinal epithelial cells retain, after demembranation in presence calcium, two major proteins (I, II) which are released by addition calcium chelators. We have purified and characterized these calcium-binding proteins. Protein I has a mol. wt. 85 000 contains copies 36-K subunit an additional 10-K subunit. It binds calcium-dependent manner to F-actin as well non-erythroid spectrin. Immunofluorescence microscopy reveals protein I-related antigens terminal web cell submembraneous cortical layer various tissue culture cells. Biochemical immunological results document that is identical with cellular p36K recognized substrate for tyrosine phosphorylation sarc gene kinase Rous sarcoma virus-transformed The biochemical properties agree its location seen immunofluorescence fractionation suggest actin-spectrin network may be affected virus transformation.
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