Acid Phosphatases in Germinating Lettuce — Evidence for Partial Activation
- 1 February 1971
- journal article
- Published by Wiley in Physiologia Plantarum
- Vol. 24 (1) , 95-101
- https://doi.org/10.1111/j.1399-3054.1971.tb06724.x
Abstract
At least nine acid phosphatases and a distinct phytase are present in different cell fractions of germinating lettuce. The enzymes could be partially characterised using acrylamide gel electrophoresis. Phosphatase formation is only partially inhibited by cycloheximide. A new soluble ATPase arises between 24 and 48 hours of germination. Its formation is not inhibited by cycloheximide. Phosphatase activity in the particulate fraction of the cell can be liberated and activated by detergent or trypsin treatment. It is suggested that the newly formed soluble ATPase arises by release and activation of a particulate phosphatase.Keywords
This publication has 14 references indexed in Scilit:
- THE COLORIMETRIC DETERMINATION OF PHOSPHORUSPublished by Elsevier ,2021
- Incorporation in vivo of 14C-Labelled Amino Acids into the Proteins of Mitochondrial Ribosomes from Neurospora crassa Sensitive to Cycloheximide and Insensitive to ChloramphenicolEuropean Journal of Biochemistry, 1969
- ADP KINASE AND ATPASE IN CHLOROPLASTSProceedings of the National Academy of Sciences, 1969
- Early effects of gibberellic acid on barley aleurone layersBiochemical and Biophysical Research Communications, 1968
- Activation of enzymes during germination—trypsin-like enzyme in lettucePhytochemistry, 1968
- The Effect of Cycloheximide (Actidione) on Protein and Nucleic Acid Synthesis byChlorellaJournal of Experimental Botany, 1967
- Proteolytic Enzymes and Endogenous Trypsin Inhibitor in Germinating Lettuce SeedsPhysiologia Plantarum, 1965
- Partial Resolution of the Enzymes Catalyzing PhotophosphorylationJournal of Biological Chemistry, 1965
- ELECTROPHORETIC SEPARATION OF MULTIPLE FORMS OF PARTICLE ASSOCIATED ACID PHOSPHATASEAnnals of the New York Academy of Sciences, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964