Biography:

In the past Benjamin Preiss has collaborated on articles with Jean-Guy Lehoux and BENJAMIN PREISS. One of their most recent publications is Short communicationOn the lack of acetoacetate formation in some amphibian livers. Which was published in journal Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism.

More information about Benjamin Preiss research including statistics on their citations can be found on their Copernicus Academic profile page.

Benjamin Preiss's Articles: (7)

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

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.

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

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.

A comparative study of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in vertebrate adrenocortical tissues

AbstractOur study compares the activities in vitro of HMG-CoA reductase in hamster, rabbit, rat, chicken, and frog adrenocortical tissues. Microsomal and mitochondrial preparations obtained by differential centrifugation were incubated with [3-14C]HMG-CoA and a NADPH generating system, and the [14C]mevalonic acid formed was isolated on a silica gel column and by thin-layer chromatography. The identity of the product was confirmed by formation of the benzhydrylamide derivative followed by crystallization to constant isotope ratio. The following adrenocortical HMG-CoA reductase activities were found (nanomoles of mevalonic acid formed per milligram of protein per 30 min): hamster microsomal fraction, 19.3; hamster mitochondrial fraction, 15.1; rabbit microsomal fraction, 2.8; rat microsomal fraction, 0.35; chicken microsomal fraction, 7.4; chicken mitochondrial fraction, 3.4; and frog microsomal fraction, 0.14. Our results suggest that the ability of various adrenocortical tissues to synthetize cholesterol is related to the level of HMG-CoA reductase activity present.

Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!

Contact us