Proteinase involvement in the solubilization of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
作者： Gene C. Ness , Sue C. Way , Pat S. Wickham
DOI: 10.1016/0006-291X(81)91491-1
关键词: Reductase 、 Chemistry 、 Leupeptin 、 Thiol 、 Phenylmethylsulfonyl Fluoride 、 PMSF 、 Pepstatin 、 Antipain 、 HMG-CoA reductase 、 Biochemistry
摘要: Abstract This paper demonstrates that a heavy particle fraction, which contains lysosomes, is required for the solubilization of HMG-CoA reductase from rat liver microsomes by widely-used slow freeze-thaw procedure. effectively inhibited proteinase inhibitors, leupeptin and antipain, but not phenylmethylsulfonyl fluoride, pepstatin A or N-α-p-tosyl-L-lysine methyl ester. These results suggest thiol proteinase, possibly derived responsible solubilizing reductase.
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