Hydroxymethylglutaryl coenzyme A reductase activity in hamster adrenal mitochondria purified on a sucrose gradient
Review articleOpen access

AbstractHamster adrenal homogenates were fractionated by differential centrifugation to obtain crude mitochondrial and microsomal pellets. The mitochondria were further purified on a linear sucrose density gradient. The crude mitochondrial fraction was separated into three bands on the gradient. One of the bands (band 3, D2020 = 1.165) contained all the measurable cytochrome C oxidase activity. Band 3 also contained the highest specific activity of HMG-CoA reductase corresponding to a 1.9 fold enrichment compared to the crude mitochondrial pellet. The evidence presented supports the possibility that a part of the HMG-CoA reductase activity in hamster adrenals is associated with mitochondria.

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