Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin
作者： R A Kahn , A G Gilman
DOI: 10.1016/S0021-9258(20)82130-9
关键词: G alpha subunit 、 GTP' 、 Cholera toxin 、 Cell biology 、 ADP-ribosylation 、 Biology 、 ADP ribosylation factor 、 Biochemistry 、 Cyclase activity 、 Adenylate kinase 、 Cyclase
摘要: A factor (ARF) that is required for the cholera toxin-dependent ADP-ribosylation of the stimulatory, GTP-binding regulatory component (Gs) of adenylate cyclase has been purified about 2000-fold from cholate extracts of rabbit liver membranes. ARF is an intrinsic membrane protein with Mr= 21,000. The final product can be resolved into two polypeptides with very similar molecular weights; each of these has ARF activity. The ADP-ribosylation of Gs can now be studied with defined components. GTP and ARF are both necessary …
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