Abstract
Exposures of intact rat liver microsomes to various sulfhydryl reagents or to concentrations of taurocholate below 1 mM inhibited glucose 6-phosphate phosphohydrolase activity. The inhibitions were abolished by subsequent disruption of membrane integrity by higher concentrations of taurocholate or 1M NH 4OH. Also the reagents were ineffective when tested directly with disrupted microsomes. Thus, a requirement for an intact membrane structure in the action of these reagents is indicated. Moreover, the involvement of a second component of the endoplasmic reticulum in the catalysis of glucose 6-phosphate hydrolysis is suggested.
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