Aspergillus Proteinaseに関する研究(第2報) : Aspergillus melleus 産生する微アルカリプ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38報

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A semi-alkaline proteinase of Aspergillus melleus has been purified approximately 15.7-fold from a culture extract by pH treatment, lead subacetate treatment, decolorization with Amberlite IRA93,fractionation with ethanol and ammonium sulfate, dialysis, treatment with acrinol and acid clay, precipitation with acetone, and gel-filtration on Sephadex G75. The purified proteinase obtained as needle crystals or pillar-shaped crystals was monodisperse in both the ultracentrifugation pattern and the moving-boundary electrophoresis. The optimum pH and temperature for the activity were 8 and 50°, respectively. At 20°, the enzyme was highly stable at the range of pH 5 to 9. Metallic salts except HgCl_2,AgNO_3 and FeCl_3,sulfhydryl reagent, reducing and oxidizing reagents tested had no effect on the activity, but potato trypsin inhibitor, soy-bean trypsin inhibitor, di-isopropyl-fluorophosphate and N-bromosuccinimide caused a marked inhibition.
公益社団法人日本薬学会の論文
1968-12-25