Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase
- 15 January 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 217 (2), 499-505
- https://doi.org/10.1042/bj2170499
Abstract
Acylphosphatase (acylphosphate phosphohydrolase, EC 3.6.1.7) was purified from guinea-pig muscle by a procedure involving immuno-affinity chromatography and a subsequent ion-exchange chromatography. This purification technique gave an overall yield of .apprx. 60% and permitted the isolation of 3 molecular forms with acylphosphatase activity, with a distribution greatly resembling those found in horse and turkey muscle. The main form appears to be very similar to the corresponding form in horse and turkey muscle, as indicated by amino acid composition, end-group analysis, the presence of glutathione as a mixed disulfide in almost the same stoichiometric ratio and kinetic analysis. From turnover data, the main form of acylphosphatase in guinea-pig muscle exhibits a degradation constant of 0.10 day-1, corresponding to a half-life of 6.8 days. These values are very close to those found for muscle total soluble proteins.This publication has 18 references indexed in Scilit:
- Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediateArchives of Biochemistry and Biophysics, 1981
- A new synthesis of benzoyl phosphate: A substrate for acyl phosphatase assayCellular and Molecular Life Sciences, 1976
- A general procedure for the manual sequencing of small quantities of peptidesAnalytical Biochemistry, 1975
- [64] 1,3-Diphosphoglycerate phosphataseMethods in Enzymology, 1975
- A histone protease of rat liver chromatinBiochemical and Biophysical Research Communications, 1972
- Preliminary studies on horse muscle acylphosphatase structure. Evidence of a mixed disulfide with glutathioneBiochemistry, 1971
- Horse muscle acyl phosphatase: Purification and some propertiesArchives of Biochemistry and Biophysics, 1969
- High resolution acrylamide gel electrophoresis of histonesArchives of Biochemistry and Biophysics, 1969
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959
- Purification and properties of brain carbamyl and acyl phosphataseBiochimica et Biophysica Acta, 1958