Association of Enzymatic Activity with Submicroscopic Particles
- 9 May 1952
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 115 (2993) , 521-522
- https://doi.org/10.1126/science.115.2993.521
Abstract
Considerable study of the mitochondrial fraction of tissues has shown that these particulates possess the major portion of the activity of a number of tissue enzyme systems. Previous studies have not indicated,however, exclusive localization of an enzymatic activity in these particles. Investigations on the hydrolysis of triacetic acid lactone by rat kidney homogenates revealed that almost all of the lactonase activity could be sedimented and fractionated, indicating that about 70% of this activity was associated with the submicroscopic particles, whereas the mitochondrial fraction possessed approx. 7% of the total activity. Since the slight activity of the mitochondrial fractions can probably be attributed to contamination by submicroscopic particles, it is suggested that the lactonase activity is an exclusive function of microsomes.Keywords
This publication has 10 references indexed in Scilit:
- INTRACELLULAR DISTRIBUTION OF ENZYMESJournal of Biological Chemistry, 1950
- Studies on mitochondria: II. The structure of mitochondria in relation to enzymatic activityExperimental Cell Research, 1950
- Studies on mitochondria: I. The association of cyclophorase with mitochondriaExperimental Cell Research, 1950
- THE SEPARATION OF DEHYDROPEPTIDASE AND ANALOGOUS l- AND d-PEPTIDASESJournal of Biological Chemistry, 1949
- Lactonase and C-Acylase Activity of HepatomaJNCI Journal of the National Cancer Institute, 1949
- METABOLISM OF 3,5-DIKETOHEXANOIC ACID AND ITS δ-LACTONE BY TISSUE HOMOGENATESPublished by Elsevier ,1949
- METABOLISM OF 3,5-DIKETOHEXANOIC ACID AND ITS DELTA-LACTONE BY TISSUE HOMOGENATES1949
- INTRACELLULAR DISTRIBUTION OF ENZYMESPublished by Elsevier ,1946
- INTRACELLULAR DISTRIBUTION OF ENZYMES .1. THE DISTRIBUTION OF SUCCINIC DEHYDROGENASE, CYTOCHROME OXIDASE, ADENOSINETRIPHOSPHATASE, AND PHOSPHORUS COMPOUNDS IN NORMAL RAT TISSUES1946