Heparin inhibits the activity of protein phosphatase‐1
Open Access
- 9 April 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 169 (1) , 45-48
- https://doi.org/10.1016/0014-5793(84)80286-0
Abstract
Heparin inhibited the dephosphorylation of rabbit skeletal muscle or liver phosphorylase a by protein phosphatase‐1. Other glycosaminoglycans (chondroitin sulfates) and their constituents were found to be without effect. The chromatography of a partially purified phosphatase preparation on heparin—Sepharose CL‐6B resulted in a fraction that did not bind to the matrix and its activity was not inhibited by heparin or inhibitor‐1. The phosphatase bound to heparin—Sepharose was eluted by 0.2 M NaCl and was inhibited by heparin or inhibitor‐1.Keywords
This publication has 17 references indexed in Scilit:
- Characterisation of a Reconstituted Mg‐ATP‐Dependent Protein PhosphataseEuropean Journal of Biochemistry, 1983
- Heterotropic interactions of AMP and glucose binding sites in phosphorylase a are destroyed by limited proteolysisBiochemical and Biophysical Research Communications, 1983
- A Kinetic Analysis of the Effects of Inhibitor-1 and Inhibitor-2 on the Activity of Protein Phosphatase-1European Journal of Biochemistry, 1983
- Glycogen Synthase from Rabbit Skeletal MuscleEuropean Journal of Biochemistry, 1982
- The role of protein phosphorylation in neural and hormonal control of cellular activityNature, 1982
- Interconvertible Enzyme Cascades in Cellular RegulationAnnual Review of Biochemistry, 1980
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- The Rigulation of Glycogen MetabolismEuropean Journal of Biochemistry, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970