Purification of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from rat liver.
- 1 April 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (4) , 1431-1435
- https://doi.org/10.1073/pnas.74.4.1431
Abstract
A procedure for the purification of 3-hydroxy-3-methylglutaryl-coenzyme A reductase [mevalonate:NADP+ oxidoreductase (CoA-acylating); EC 1.1.1.34] solubilized from rat liver microsomes is reported. This enzyme has a specific activity of 9000-10,000 nmol of mevalonate formed per min/mg of protein. This represents a 4100-fold purification over the activity in microsomes, and a specific activity that is approximately 20-fold greater than the highest previously reported value. The enzyme is judged to be homogeneous on the basis of sodium dodecyl sulfate/polyacrylamide disc gel electrophoresis, polyacrylamide disc gel electrophoresis and immunoanalysis. Data are also presented that indicate the separation of enzymatically active and inactive species of 3-hydroxy-3-methylglutaryl-coenzyme A reductase on affinity chromatography on a coenzyme A column.This publication has 21 references indexed in Scilit:
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