The control of phosphorylase kinase phosphatase by “second site phosphorylation”; A new form of enzyme regulation
- 1 August 1973
- journal article
- Published by Wiley in FEBS Letters
- Vol. 34 (1) , 43-47
- https://doi.org/10.1016/0014-5793(73)80699-4
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- The Subunit Structure of Rabbit‐Skeletal‐Muscle Phosphorylase Kinase, and the Molecular Basis of Its Activation ReactionsEuropean Journal of Biochemistry, 1973
- Activation of glycogen synthetase and inactivation of phosphorylase kinase by the same phosphoprotein phosphataseBiochemical and Biophysical Research Communications, 1973
- Physicochemical properties of rabbit skeletal muscle phosphorylase kinaseBiochemistry, 1973
- Subunit structure of rabbit skeletal muscle phosphorylase kinaseBiochemistry, 1973
- Activation and phosphorylation of the subunits of phosphorylase kinaseBiochemical Journal, 1972
- α-Keto acid dehydrogenase complexesArchives of Biochemistry and Biophysics, 1972
- Molecular characteristics of the totally dependent and independent forms of glycogen synthase of rabbit skeletal muscle: II. Some chemical characteristics of the enzyme protein and of its change on interconversionBiochimica et Biophysica Acta (BBA) - Enzymology, 1971
- The Regulation of Skeletal Muscle Phosphorylase Kinase by Ca2+Journal of Biological Chemistry, 1971
- Reversal of Phosphorylase Kinase ActivationJournal of Biological Chemistry, 1968
- Reversible Stimulation of Muscle Phosphorylase b Kinase by Low Concentrations of Calcium IonsThe Journal of Biochemistry, 1967