Subcellular localization of 3-hydroxy-3-methylglutaryl coenzyme A reductase and other membrane-bound enzymes in sweet potato roots1
- 1 August 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 17 (4) , 691-700
- https://doi.org/10.1093/oxfordjournals.pcp.a075325
Abstract
The subcellular localization of 3-hydroxy-3-methylglutaryl coenzyme A reductase and other membrane-bound enzymes in fresh, cut and diseased sweet potato root tissues was resolved by differential centrifugation and sucrose density gradient centrifugation. In fresh, cut and diseased tissues, cytochrome c oxidase was almost localized in mitochondria, and NADH cytochrome c reductase was in mitochondria in fresh and cut tissues, but in both mitochondria and microsomes in diseased tissue. NADPH cytochrome c reductase and antimycin A insensitive NADH cytochrome c reductase were mainly associated with microsomes. Catalase was dominantly found in the mitochondrial fraction. 3-Hydroxy-3-methylglutaryl coenzyme A reductase was localized only in mitochondria and not in microsomal and supernatant fractions in both fresh and cut tissues. In diseased tissue (infected with Ceratocystis fimbriata), in addition to being present in mitochondria, the enzyme was also localized in microsomes. These results indicate that microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase whose activity rapidly increased in response to the infection, predominandy participates in the formation of terpenes such as ipomeamarone.This publication has 5 references indexed in Scilit:
- THE LARGE-SCALE SEPARATION OF PEROXISOMES, MITOCHONDRIA, AND LYSOSOMES FROM THE LIVERS OF RATS INJECTED WITH TRITON WR-1339The Journal of cell biology, 1968
- Studies on the Phospholipid Requirement of Glucose 6-PhosphataseJournal of Biological Chemistry, 1968
- IPOMEAMARONE ACCUMULATION AND LIPID METABOLISM IN SWEET POTATO INFECTED BY THE BLACK ROT FUNGUS I. IDENTIFICATION OF STEROL AND CHANGES IN LIPID METABOLISM DURING INFECTION PROCESS1Plant and Cell Physiology, 1964
- METHYLGLUTACONASE, EINE NEUE HYDRATASE, DIE AM STOFFWECHSEL VERZWEIGTER CARBONSAUREN BETEILIGT IST1958
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951