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Wiley, FEBS Letters, 2(362), p. 101-105, 1995

DOI: 10.1016/0014-5793(95)00197-h

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Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

Journal article published in 1995 by Greg Moorhead, Carol MacKintosh ORCID, Nick Morrice, Philip Cohen
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The form of protein phosphatase-l associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration, The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the alpha and beta isoforms) complexed to a 33 kDa glycogen-binding (G(L)) subunit. The G(L) subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.