[39] Protein phosphatase-2C from rabbit skeletal muscle and liver: An Mg2+-dependent enzyme
- 1 January 1988
- book chapter
- Published by Elsevier in Methods in Enzymology
- Vol. 159, 416-426
- https://doi.org/10.1016/0076-6879(88)59041-9
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Primary structure analysis proves that protein phosphatases 2C1 and 2C2 are isozymesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1987
- Identification of two isoenzymes of protein phosphatase 2C in both rabbit skeletal muscle and liverEuropean Journal of Biochemistry, 1987
- Protein Phosphatases: Properties and Role in Cellular RegulationScience, 1983
- The Protein Phosphatases Involved in Cellular Regulation. 1. Classification and Substrate SpecificitiesEuropean Journal of Biochemistry, 1983
- The Protein Phosphatases Invloved in Cellular Regulation. 4. Classification of Two Homogeneous Myosin Light Chain Phosphatases from Smoth Muscle as Protein Phosphatase-2A1 and 2C, and a Homogeneous Protein Phosphatase from Reticulocytes Active on Protein Synthesis Initiation Factor eIF-2 as Protein Phosphatase-2A2European Journal of Biochemistry, 1983
- Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulinBiochemistry, 1980
- Isolation of cardiac myofibrils and myosin light chains with in vivo levels of light chain phosphorylationBiochimica et Biophysica Acta (BBA) - General Subjects, 1979
- The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal MuscleEuropean Journal of Biochemistry, 1979
- 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