麹菌の生産するプロテアーゼ : I. Taka-proteaseの分画

概要

論文の詳細を見る
According to the procedure listed in Fig. 1(p. 308), the acid protease preparation (fraction 2) was obtained from the commercial preparaton of Taka-diastase. By zone electrophoresis of pH 6 using starch as supporting substance, the preparation could be devided into two distinct fractions ; one which moved toward the anode was named acid protease I, and the other found in the cathode side acid protease II. A small amount of other protease contained in the latter fraction colud be inactivated by incubating the enzyme solution at pH 3. Both fractions, acid proteases I and II, have the same optimum pH at 3,but the two differ distinctly from each other in the inhibition patterns with sodium laurylsulfonate (SLS) and ethylenediamine tetraacetate (EDTA) as inhibitors (Fig. 8 and 9,p. 310). From the fraction 2,was obtained a protease fraction having an optimum pH at 7 after the acid proteases being inactivated by incubating at pH 7. This fraction, named neutral protease II, differs from the neutral protease already known (neutral protease I) in precipitability with rivanol, adsorption as well as electrophoretic behaviors and sensitivity to EDTA and pototo inhibitor as shown in Table 3. Tests for the existence of semi-acid protease (opt. pH : 6) which had been postulated by MATSUSHIMA led to the negative results, and the activty-pH curves seemingly suggesting its existence with casein as substrate, especially in the presence of SLS, were fully discussed.
1960-07-15

麹菌の生産するプロテアーゼ : I. Taka-proteaseの分画

スポンサーリンク

概要

著者

関連論文

スポンサーリンク