Aspergillus Proteinaseに関する研究(第1報) : Aspergillus melleusの産生するアルカリブロティナーゼの精製結晶化ならびに酵素化学的性質について酵素剤の研究第37報

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An alkaline proteinase of Aspergillus melleus has been purified approximately 11.2-fold from a culture extract by treatment with lead subacetate, fractionation with ammonium sulfate, treatment with acrinol, fractionation with acetone, and gel-filtration on Sephadex G75. The purified proteinase obtained as pillar-shaped crystals was monodisperse in both the ultracentrifugation and the moving-boundary electrophoresis. The optimum pH and temperature for the activity were 9 and 52°, respectively. At 20°, the enzyme was highly stable at the range of pH 4.5 to 9.5. At pH 7,the activity was lost at 65° within ten minutes. None of the metallic salts tested increased the activity, but Hg^<2+> and Ag^+ were found to be inhibitory. Sulfhydryl reagent, reducing and oxidizing reagents tested had no effect on the activity, but potato trypsin inhibitor, di-isopropyl-fluorophosphate and soy-bean trypsin inhibitor caused a marked inhibition.
公益社団法人日本薬学会の論文
1968-12-25