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- W4256013676 abstract "Some experiments were carried out with purified neutral proteinases I and II of Aspergillus sojae in relation to their characteristics as metalloenzyme. The both enzymes contained one gram atom of zinc and about two gram atoms of calcium per mole (molecular weights of 41,700 for I and 19,800 for II were estimated by gel filtration) of enzyme protein, and the zinc was essential for the activity. Some metal-chelating agents, such as ethylenediaminetetraacetic acid (EDTA), o-phenanthroline, 8-hydroxyquinoline and α,α′-dipyridyl, inhibited the activity of the both enzymes. In the inactivation of neutral proteinase II by EDTA a distinct pH-dependency was observed. The EDTA-inactivated enzymes were reactivated fully or partially by the addition of some metal ions such as Zn2+, Co2+, Mn2+, Cu2+ (only neutral proteinase II) and Ni2+. Zinc-free apo-enzymes were prepared from the native enzymes by the dialysis against EDTA solution. The apo-enzyme of neutral proteinase I still contained calcium, while that of neutral proteinase II did not. The apo-enzymes restored their activity for the most part either by the addition of excess amount of zinc or by mixing with a stoichiometric amount of zinc in the presence of calcium at an alkaline condition." @default.
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- W4256013676 date "1972-12-01" @default.
- W4256013676 modified "2023-09-26" @default.
- W4256013676 title "Some Properties of Neutral Proteinases I and II ofAspergillus sojaeas Zinc-containing Metalloenzyme" @default.
- W4256013676 doi "https://doi.org/10.1080/00021369.1972.10860530" @default.
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