Journal of Lipid Research, Vol 23, 523-530, Copyright © 1982 by Lipid Research, Inc.
Purification of 3-hydroxy-3-methylglutaryl coenzyme A reductase from human liver
RD Tanaka, PA Edwards, SF Lan, EM Knoppel and AM Fogelman
The enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase from human liver
was purified to homogeneity. Electrophoresis of the purified human enzyme
on non-denaturing gels revealed a single protein-staining band that
co-migrated with reductase activity and could be selectively removed by
treatment with cross-reacting antibody prepared to the purified reductase
from rat liver. On SDS polyacrylamide gel electrophoresis, the purified
reductase showed only one protein- staining band corresponding to a
molecular weight of approximately 52,000. Based on the sedimentation rate
during sucrose density gradient centrifugation, most of the enzyme from
crude solubilized preparations had an apparent molecular weight of
approximately 104,000. The human reductase, like the rat liver enzyme, was
dimeric and composed of subunits of approximately 50,000 molecular weight.
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