Purification of a membraneous actin binding protein from bovine adrenal medulla.
An actin binding protein having a molecular mass of 39,000 was purified from the Triton extract of bovine adrenal medulla membrane fraction using DNase I affinity column and following chromatographies. Specific antibody was produced against the protein and immunoblotting analysis of tissue extract showed the purified protein was not a breakdown product of a larger protein and also showed the presence of this protein in bovine adrenal medullary chromaffin cells and rat pheochromocytoma cells (PC12). An immunoblotting analysis of membrane fractions treated with nucleotides and their analogues showed that this protein was specifically solubilized in the presence of GTP gamma-S.
Maekawa
S
S
Department of Biochemistry, Faculty of Science, University of Tokyo, Japan.
D000199:Actins / Q000378:metabolism; D000313:Adrenal Medulla / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D007120:Immunochemistry; D066298:In Vitro Techniques; D008566:Membranes / Q000737:chemistry; D008840:Microfilament Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009711:Nucleotides / Q000378:metabolism; D012995:Solubility
D000199:Actins; D008840:Microfilament Proteins; D009711:Nucleotides