Updated Protocols and Comments on the Purification without Use of Activating Ligands of the Coupling Proteins Nsand Niof the Hormone Sensitive Adenylyl Cyclase

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Abstract
Ns and Ni have been purified without using NaF and Mg as stabilizing agents (Codina, J., Hildebrandt, J.D., Sekura, R.D., Birnbaumer, M., Bryan, J., Manclark, C.R. and Birnbaumer, L. [1984] J. Biol. Chem. 259, in press). Since the submission of that report, several modifications have been introduced to the purification procedure and additional fractions have been processed from which N proteins are obtained. This article describes the updated protocols and presents methodological details not included in the previous publication. The final products are Ns, the stimulatory N, Ni the inhibitory N, both of subunit structure αβγ, and a Mr=40,000 protein of βγ composition. They are obtained from human erythrocytes.