Schell H D, Mateescu M A
Acta Biol Med Ger. 1975;34(6):959-63.
The properties of peroxidase insolubilized by covalent binding to CH- and AH-Sepharose 4 B in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) are described. CH-Sepharose 4 B bound peroxidase yields an enzyme preparation with a residual specific activity of 60.6%. When bound to AH-Sepharose 4 B, the residual specific activity is to 78%. The reasons of these differences in the catalytic activity of the two insolubilized enzyme preparations are discussed. By covalent binding on CH- and AH-Sepharose 4 B, peroxidase exibits no changes in its pH optimum; it virtually keeps the same activity after being used ten times. Insolubilized peroxidase preparations, dried and reimbibed after being stored for 6 weeks at room temperature still display 50% of the initial specific activity of the insolubilized enzyme. Stored in acetate buffer, the enzyme preparations maintain their activity during all this interval.
本文描述了在1-乙基-3-(3-二甲基氨基丙基)碳二亚胺（EDC）存在下，通过共价结合到CH-和AH-琼脂糖4B上而固定化的过氧化物酶的性质。CH-琼脂糖4B结合的过氧化物酶产生的酶制剂残余比活性为60.6%。当结合到AH-琼脂糖4B上时，残余比活性为78%。讨论了两种固定化酶制剂催化活性存在这些差异的原因。通过共价结合到CH-和AH-琼脂糖4B上，过氧化物酶的最适pH没有变化；使用十次后其活性基本保持不变。固定化的过氧化物酶制剂在室温下储存6周后干燥并重新水化，仍显示出固定化酶初始比活性的50%。储存在醋酸盐缓冲液中，酶制剂在整个这段时间内都保持其活性。
