Possible isoenzymes of monoamine oxidase in rat tissues
- 1 April 1968
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 46 (4) , 295-297
- https://doi.org/10.1139/o68-044
Abstract
The solubilized monoamine oxidase activity of rat liver, kidney, and brain can be separated into several bands by cellulose polyacetate membrane electrophoresis. Four such bands of activity are found in the whole liver homogenate while mitochondrial and microsomal fractions appear to have two. The activity of these bands has been assayed using three different substrates, isoamylamine, tyramine, and benzylamine. The solubilized mitochondrial monoamine oxidase activity of kidney and brain when submitted to electrophoresis is found to separate in two fractions. There is some small but consistent difference of distribution of activity when using different substrates.This publication has 9 references indexed in Scilit:
- THE ACTIVITY OF LACTATE DEHYDROGENASE ISOZYMES DURING THYROXINE-INDUCED TADPOLE METAMORPHOSISCanadian Journal of Biochemistry, 1966
- Anion inhibition of monoamine oxidaseBiochemical Pharmacology, 1966
- The study of monoamine oxidase activity by histochemical proceduresBiochemical Pharmacology, 1965
- MONOAMINE OXIDASE - PURIFICATION, CRYSTALLIZATION, AND PROPERTIES OF PLASMA MONOAMINE OXIDASE1962
- Oxydation von serotonin und tyramin durch rattenlebermitochondrienBiochimica et Biophysica Acta, 1961
- INHIBITION OF AMINE OXIDASE BY METAL IONS AND BY SULPHYDRYL COMPOUNDSCanadian Journal of Biochemistry and Physiology, 1956
- AMINE OXIDASE AND AMINE METABOLISM1952
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- INTRACELLULAR DISTRIBUTION OF ENZYMES .3. THE OXIDATION OF OCTANOIC ACID BY RAT LIVER FRACTIONS1948