Subcellular localization of acid proteinase in barley mesophyll protoplasts
- 1 February 1981
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 151 (2) , 198-200
- https://doi.org/10.1007/bf00387823
Abstract
Chloroplasts prepared from lysed protoplasts of barley mesophyll contain 2–8% of the total acid proteinase activity. This residual activity is not associated with intact chloroplasts isolated by means of density gradient centrifugation. Vacuoles isolated from lysed protoplasts contain 80–85% of the total acid proteinase activity, indicating that the enzyme(s) which is presumably responsible for the degradation of chloroplastic proteins is located largely in the central vacuoles of mesophyll cells.This publication has 12 references indexed in Scilit:
- Vacuoles as storage compartments for nitrate in barley leavesNature, 1981
- Plastid Protease Activity and Prolamellar Body Transformation during GreeningPlant Physiology, 1980
- Azocoll-digesting Proteinases in Soybean LeavesPlant Physiology, 1979
- Hydrolytic Enzymes in the Central Vacuole of Plant CellsPlant Physiology, 1979
- Breakdown of Ribulose Bisphosphate Carboxylase and Change in Proteolytic Activity during Dark-induced Senescence of Wheat SeedlingsPlant Physiology, 1978
- Refinement of the Coomassie blue method of protein quantitationAnalytical Biochemistry, 1978
- Loss of Ribulose 1,5-Diphosphate Carboxylase and Increase in Proteolytic Activity during Senescence of Detached Primary Barley LeavesPlant Physiology, 1975
- The determination of amino-acids with ninhydrinThe Analyst, 1955
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARISPlant Physiology, 1949