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- W2113130514 abstract "Both the catalytic protein (C) and the guanine nucleotide-binding regulatory protein (G/F) of rabbit hepatic adenylate cyclase were solubilized in active form in sodium cholate at high ionic strength. Upon precipitation by (NH4)SO4, C was selectively aggregated such that it was largely excluded from Ultrogel AcA 34 when chromatographed in cholate solution at high ionic strength. G/F eluted with KD congruent to 0.5. Thus C can be completely resolved from G/F by this procedure. Rabbit hepatic C prepared in this way resembles the C activity previously described by us in the cyc- mutant of S49 lymphoma cells (Ross, E. M., Howlett, A. C., Ferguson, K. M., and Gilman, A. G. (1978) J. Biol. Chem. 253, 6401-6412). Similarities include 7- to 10-fold stimulation by Mn2+ relative to Mg2+ and a complete lack of sensitivity to fluoride or guanine nucleotides. Reconstitution of hepatic C with hepatic G/F causes restoration of stimulation up to 25-fold by either of these activators in the presence of Mg2+. While C is relatively unstable in cholate under these conditions, especially at temperatures over 4 degrees C, it is stabilized by removal of cholate and by addition of phospholipid. These procedures allow the study of the catalytic protein of adenylate cyclase from a hormone-responsive tissue in the absence of endogenous regulatory protein or membrane lipid and also provide a starting point for the purification of the catalyst." @default.
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- W2113130514 date "1981-02-01" @default.
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- W2113130514 title "Physical separation of the catalytic and regulatory proteins of hepatic adenylate cyclase." @default.
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- W2113130514 doi "https://doi.org/10.1016/s0021-9258(19)69899-6" @default.
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