Ugarova N N, Kershengol'ts B M, Artomonov I D, Berezin I V
Biokhimiia. 1976 Oct;41(10):1829-36.
Pretreatment of peroxidase by its covalent coupling to inert proteins and albumin by means of glutaraldehyde considerably increases the thermostability and specific activity of polyacrylamide gel (PAAG) immobilized peroxidase. The effects of PAAG composition on the catalytic properties of the immobilized oligomers: peroxidase-inert proteins-albumin, are studied. The oligomers immobilized in 40% PAAG (10% N,N'-methylenebisacrylamide) possess the maximal specific activity (4.5 nmol/g). The effects of oligomer composition on their catalytic activity and stability in PAAG are studied. The stability of oligomers of optimal composition (ratio of albumin/peroxidase is 2.4), incorporated into 40% PAAG, is 15 times higher as compared to that of the soluble enzyme and 250 times higher as compared to that of the enzyme incorporated into PAAG without pretreatment. A mechanism of stabilizing effect exerted by albumin on peroxidase in PAAG-immobilized oligomers, is discussed.
通过戊二醛将过氧化物酶与惰性蛋白质和白蛋白共价偶联进行预处理，可显著提高聚丙烯酰胺凝胶（PAAG）固定化过氧化物酶的热稳定性和比活性。研究了PAAG组成对固定化低聚物：过氧化物酶 - 惰性蛋白质 - 白蛋白催化性能的影响。固定在40% PAAG（10% N，N'-亚甲基双丙烯酰胺）中的低聚物具有最大比活性（4.5 nmol/g）。研究了低聚物组成对其在PAAG中的催化活性和稳定性的影响。掺入40% PAAG中的最佳组成低聚物（白蛋白/过氧化物酶比例为2.4）的稳定性，与可溶性酶相比高15倍，与未经预处理掺入PAAG中的酶相比高250倍。讨论了白蛋白对PAAG固定化低聚物中过氧化物酶的稳定作用机制。
