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  • Title: Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1.
    Author: Doherty MJ, Moorhead G, Morrice N, Cohen P, Cohen PT.
    Journal: FEBS Lett; 1995 Nov 20; 375(3):294-8. PubMed ID: 7498521.
    Abstract:
    A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatase-1 (PP1) was isolated from a rat liver library. The deduced amino acid sequence (284 residues, 32.6 kDa) was 23% identical (39% similar) to the N-terminal region of the glycogen-binding (GM) subunit of PP1 from striated muscle. The similarities between GM and GL were most striking between residues 63-86, 144-166 and 186-227 of human GM (approximately 40% identity), nearly all the identities with the putative yeast homologue GAC1 being located between 144-166 and 186-227. The cDNA was expressed in E. coli, and the expressed protein transformed the properties of PP1 to those characteristic of the hepatic glycogen-associated enzyme. These experiments establish that the cloned protein is GL.
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