Purification of rabbit skeletal muscle protein kinase regulatory subunit using cyclic adenosine-3':5'-monophosphate affinity chromatography.

作者: William L. Dills , Joseph A. Beavo , Peter J. Bechtel , Edwin G. Krebs

DOI: 10.1016/S0006-291X(75)80406-2

关键词:

摘要: Summary A method for the preparation of homogeneous protein kinase regulatory subunit has been developed using adenosine-3′,5′-monophosphate (cAMP) affinity chromatography. N 6 -(2-Aminoethyl)-cAMP was synthesized and covalently linked to CNBr-activated Sepharose 4B. When a crude rabbit skeletal muscle applied ge1, cAMP independent activity recovered in effluent. The bound not removed with 2 M NaC1 but could be eluted 30 mM cAMP. This identical prepared by other methods as judged electrophoretic migration presence sodium dodecylsulfate, binding, inhibition catalytic absence

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