Evidence for the participation of two soluble noncatalytic proteins in hepatic microsomal cholesterol synthesis |
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Authors: | R C Johnson S N Shah |
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Institution: | Brain-Behavior Research Center Sonoma State Hospital Eldridge, California 95431 USA |
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Abstract: | The capacity of liver soluble fraction to stimulate hepatic microsomal conversion of squalene to cholesterol is lost on treatment with trypsin. Heat treatment of the soluble fraction results in a selective loss of its capacity to stimulate conversion of squalene to cholesterol; the ability to stimulate conversion of lanosterol and desmosterol to cholesterol is however retained. It is proposed that the liver soluble fraction contains at least two noncatalytic proteins, one heat-labile and the other heat-stable, which participate in microsomal cholesterol synthesis. The heat-labile protein mediates the conversion of squalene to lanosterol while the heat-stable protein is needed for the conversion of lanosterol and other sterol precursors to cholesterol. |
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Keywords: | To whom correspondence should be addressed |
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