Purification and characterization of c-Ki-ras p21 from bovine brain crude membranes.
作者： T Yamashita , K Yamamoto , A Kikuchi , M Kawata , J Kondo
DOI: 10.1016/S0021-9258(18)37515-X
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摘要: Abstract In the present studies, we attempted to purify native molecular forms of c-ras proteins (c-ras p21s) from bovine brain crude membranes and separated at least three GTP-binding (G proteins) cross-reactive with antibody recognizing all Ha-, Ki-, N-ras p21s. Among them, one G protein a Mr about 21,000 was highly purified characterized. The bound maximally 0.6 mol [35S]guanosine 5'-(3-O-thio)triphosphate (GTP gamma S)/mol Kd value 30 nM. [35S]GTP S-binding inhibited by GTP GDP, but not other nucleotides such as ATP, UTP, CTP. pretreatment N-ethylmaleimide. hydrolyzed liberate Pi turnover number 0.01 min-1. copurified beta subunits regulatory for adenylate cyclase. recognized against ADP-ribosylation factor Gs. peptide map different those values 25,000 20,000, designated smg p25A rho p20, respectively, which have recently membranes. partial amino acid sequence identical that human c-Ki-ras 2B p21. These results indicate is p21 in
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