Sgaragli G P, Valoti M, Della Corte L
Boll Soc Ital Biol Sper. 1984 May 30;60(5):931-5.
Peroxidase partially purified from rat intestine exhibited a tendency to aggregate which was inversely related to I values of the medium. This enzyme preparation showed an optimum pH 7.5-9.0 and was inhibited by excess H2O2 and Fe complexing agents.
从大鼠肠道中部分纯化得到的过氧化物酶表现出聚集倾向,这种倾向与介质的离子强度值呈负相关。该酶制剂的最适pH为7.5 - 9.0,并且会受到过量过氧化氢和铁络合剂的抑制。