PURIFICATION OF THE HEPATIC GLYCOGEN-ASSOCIATED FORM OF PROTEIN PHOSPHATASE-1 BY MICROCYSTIN-SEPHAROSE AFFINITY-CHROMATOGRAPHY

Authors
MOORHEAD G MACKINTOSH C MORRICE N COHEN P
Citation
G. Moorhead et al., PURIFICATION OF THE HEPATIC GLYCOGEN-ASSOCIATED FORM OF PROTEIN PHOSPHATASE-1 BY MICROCYSTIN-SEPHAROSE AFFINITY-CHROMATOGRAPHY, FEBS letters, 362(2), 1995, pp. 101-105
Citations number
33
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
362
Issue
2
Year of publication
1995
Pages
101 - 105
Database
ISI
SICI code
0014-5793(1995)362:2<101:POTHGF>2.0.ZU;2-3
Abstract
The form of protein phosphatase-l associated with hepatic glycogen (PP 1G) was purified to near homogeneity from rat liver by affinity chroma tography 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 resp onsible for the enhanced dephosphorylation of glycogen synthase by PP1 G and its allosteric inhibition by phosphorylase a.