Nakamura K, Watanabe M, Sawai-Tanimoto S, Ikeda T
Analytical and Metabolic Research Laboratories, Sankyo Co., Ltd., Tokyo, Japan.
Int J Biochem Cell Biol. 1998 Jul;30(7):823-31. doi: 10.1016/s1357-2725(98)00044-2.
Catalase was purified to an apparent homogeneity from dog erythrocytes and its properties were compared with those of human erythrocyte catalase. Purification was unsuccessful without the use of glycerol as the stabilizing agent. Molecular weight of the purified dog catalase was estimated to be about 63,000 Da in monomer and about 230,000 Da in native tetramer form. The ratio of A405/A280, the index of hematin content relative to protein, was 1.15. The isoelectric point was in the range of 5.8 to 6.4. These properties of dog catalase were very similar to those of human catalase. Dog catalase also possessed the same partial amino acid sequence as human catalase. However, the specific activity of dog enzyme was about threefold less than that of human enzyme. The amount of catalase protein in dog erythrocytes determined by immunoblotting analysis was about tenfold less than that of human erythrocytes. This was consistent with the fact that the catalase activity in dog hemolysate was about 1/30 of that in human hemolysate.
过氧化氢酶从犬红细胞中纯化至表观均一，并将其性质与人类红细胞过氧化氢酶的性质进行了比较。若不使用甘油作为稳定剂，纯化则不成功。纯化后的犬过氧化氢酶单体分子量估计约为63,000 Da，天然四聚体形式约为230,000 Da。血红素含量相对于蛋白质的指标A405/A280比值为1.15。等电点在5.8至6.4范围内。犬过氧化氢酶的这些性质与人类过氧化氢酶非常相似。犬过氧化氢酶也具有与人类过氧化氢酶相同的部分氨基酸序列。然而，犬酶的比活性约为人酶的三分之一。通过免疫印迹分析测定，犬红细胞中过氧化氢酶蛋白的量约为人类红细胞的十分之一。这与犬溶血产物中过氧化氢酶活性约为人溶血产物的1/30这一事实一致。
