Stimulation of choleragen enzymatic activities by GTP and two soluble proteins purified from bovine brain.
作者： S C Tsai , M Noda , R Adamik , P P Chang , H C Chen
DOI: 10.1016/S0021-9258(19)77942-3
关键词: GTP' 、 Cholera toxin 、 Agmatine 、 Binding protein 、 ADP ribosylation factor 、 Membrane protein 、 NAD+ kinase 、 Protein subunit 、 Molecular biology 、 Biochemistry 、 Chemistry
摘要: Choleragen (cholera toxin) activates adenylate cyclase by catalyzing ADP-ribosylation of Gs alpha, the stimulatory guanine nucleotide-binding protein. It was recently found (Tsai, S.-C., Noda, M., Adamik, R., Moss, J., and Vaughan, M. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 5139-5142) that a bovine brain membrane protein known as factor or ARF, which enhances also increases GTP-dependent NAD:arginine NAD:protein ADP-ribosyltransferase, NAD glycohydrolase, auto-ADP-ribosylation activities choleragen. We report here purification characterization two soluble proteins from similarly enhance alpha-dependent independent ADP-ribose transfer reactions catalyzed toxin. Like both factors are 19-kDA dependent on GTP analogues for activity. Maximal ARF effects were observed at molar ratio less than 2:1, ARF/toxin A subunit. Dimyristoyl phosphatidylcholine necessary optimal alpha but inhibited choleragen A1 subunit NAD:agmatine ADP-ribosyltransferase appears directly activate in fashion. The relationships to ras oncogene products family regulatory includes remains be determined.
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