Baess D, Pommerening K, Ruckpaul K
Acta Biol Med Ger. 1975;34(6):965-9.
Commerical horseradish-peroxidase was covalently bound to BrCN-activated sepharose. The activity parameters Vmax and Km were determined by the leukomalachite green reaction. Compared with the soluble enzyme, the immobilized POD has a relative residual activity of 22%. Dimethylsulfoxide and formamide were found to diminish the enzymatic activity in a concentration-dependent manner. The activity of the free enzyme in aqueous formamide solution (10%) is reduced by 43%, that of the insolubilized enzyme by 68%. Dimethylsulfoxide (15%) does not alter the LMG conversion rate of free POD, whilst a rate loss by 60% was observed for the immobilized enzyme.
将商业辣根过氧化物酶共价结合到溴化氰活化的琼脂糖上。通过白细胞孔雀绿反应测定活性参数Vmax和Km。与可溶性酶相比，固定化的过氧化物酶（POD）具有22%的相对残余活性。发现二甲基亚砜和甲酰胺以浓度依赖的方式降低酶活性。在10%甲酰胺水溶液中，游离酶的活性降低43%，固定化酶的活性降低68%。15%的二甲基亚砜不会改变游离POD的LMG转化率，而固定化酶的转化率损失60%。
