作者: Ronald E. Arebalo , Earl D. Mitchell
DOI: 10.1016/0031-9422(84)83068-X
关键词: Hydroxymethylglutaryl-CoA reductase 、 Mevalonate kinase 、 Enzyme 、 Coenzyme A 、 Differential centrifugation 、 Nepeta cataria 、 HMG-CoA reductase 、 Biology 、 Reductase 、 Biochemistry
摘要: Abstract In Nepeta cataria leaf tissue there are two separate activities of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and mevalonate (MVA) kinase respectively as determined by the use a 20–45% discontinuous sucrose density gradient. Cell-free extracts callus were prepared HMG-CoA MVA compared to in from porcine livers yeast autolysates. Callus N. has only one peak activity located at top Isolated chloroplast leaves have activity, near bottom autolysate also showed profile, Partial purification extract through differential centrifugation, 30–70% ammonium sulfate precipitation Bio-Gel P-100 column chromatography shows that kinase, 5-phosphomevalonate (MVAP) 5-pyrophosphomevalonate (MVAPP) decarboxylase remain same fractions. The extra-chloroplastidic may be separated centrifugation. These results suggest presence enzymes tissue—one second being extra-chloroplastidic.