Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00197-H/fullpdf
Reference33 articles.
1. On target with a new mechanism for the regulation of protein phosphorylation
2. The protein phosphatases involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle
3. A myofibrillar protein phosphatase from rabbit skeletal muscle contains the beta isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin
4. Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography
5. The glycogen-binding subunit of protein phosphatase-1g from rabbit skeletal muscle. Further characterisation of its structure and glycogen-binding properties
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