Iankovskiĭ O Iu, Kokriakov V N, Lyzlova S N
Ukr Biokhim Zh (1978). 1979 Sep-Oct;51(5):492-6.
Myeloperoxidase (MPO) isolated from granular fraction of cow peritoneal neutrophils had the RZ value equalled to 0.79. The absorption spectrum of MPO possesses characteristic bands at 430, 500, 570, 625, 690 nm. The molecular weight and sedimentation constant of the enzyme are 135.000-140.000 Daltons and 7.9S, respectively. The data obtained demonstrate the high thermostable property of MPO. Investigations of the pH optimum and effects of varying H2O2, o-dianizidine and MPO concentrations are described.
从牛腹膜中性粒细胞颗粒部分分离出的髓过氧化物酶(MPO)的RZ值为0.79。MPO的吸收光谱在430、500、570、625、690纳米处有特征谱带。该酶的分子量和沉降常数分别为135,000 - 140,000道尔顿和7.9S。所获得的数据表明MPO具有高热稳定性。文中描述了对最适pH以及不同过氧化氢、邻联茴香胺和MPO浓度影响的研究。