Cyclic activity of L‐asparaginase through reversible phosphorylation in Leptosphaeria michotii
Authors:
- 4 June 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 171 (1) , 67-71
Abstract
Asparaginase in L. michotii has previously been shown to have an activity rhythm, the mechanisms of which were investigated. In vitro activation, or reactivation after dephosphorylation, of the partially (200‐fold) purified asparaginase with protein kinase activity was obtained by ATP or Pi addition; these effects varied according to the phase of the activity rhythm at which enzyme was extracted. A high‐M r aggregate with asparaginase activity was phosphorylated by [γ‐32P]ATP. By SDS‐electrophoresis of dephosphorylated asparaginase a ∼60‐kDa 32P‐labelled protein with alkaline phosphatase activity became detectable. Regulation of the asparaginase activity rhythm in L. michotii is dependent on a reversible phosphorylation process.Keywords
This publication has 7 references indexed in Scilit:
- Protein Phosphatases: Properties and Role in Cellular RegulationScience, 1983
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Effects of heat shock on gene expression and subcellular protein distribution in Chinese hamster ovary cellsNucleic Acids Research, 1979
- Intestinal alkaline phosphatase. Physical properties and quaternary structureBiochemistry, 1974
- Staining of phospho-proteins on acrylamide gel electropherogramsAnalytical Biochemistry, 1973
- Separation and identification of Neurospora phosphatases by polyacrylamide gel electrophoresisAnalytical Biochemistry, 1973
- A simple and sensitive method for detection of l-asparaginase by polyacrylamide gel electrophoresisAnalytical Biochemistry, 1972