Gregory E M, Kowalski J B, Holdeman L V
J Bacteriol. 1977 Mar;129(3):1298-302. doi: 10.1128/jb.129.3.1298-1302.1977.
The catalase level of Bacteroides distasonis (ATCC 8503, type strain) varied with the amount of hemin supplied to the medium when the cells were grown in either a prereduced medium containing 0.5% peptone, 0.5% yeast extract, and 1% glucose or in a prereduced, defined heme-deficient medium. The effect of hemin on catalase production could not be duplicated by ferrous sulfate or ferrous ammonium citrate. Catalase activity reached peak values in late log phase, whereas superoxide dismutase specific activity remained constant throughout the culture growth cycle. The catalase was a nondialyzable, cyanide and azide-sensitive, heat-labile protein that coeluted with bovine erythrocyte catalase from Sepharose 6 B. Analysis of polyacrylamide gels stained for catalase activity and for heme showed a correspondence between the single catalytic activity band and one of three heme-protein bands. These data suggest a heme-protein of approximately 250,000 molecular weight. The superoxide dismutase was a cyanide-insensitive protein of approximately 40,000 molecular weight that migrated electrophoretically on acrylamide gels as a single band of activity.
当迟缓真杆菌（ATCC 8503，模式菌株）的细胞在含有0.5%蛋白胨、0.5%酵母提取物和1%葡萄糖的预还原培养基中生长，或在预还原的、明确的血红素缺陷培养基中生长时，其过氧化氢酶水平会随培养基中血红素供应的量而变化。硫酸亚铁或柠檬酸亚铁铵无法重现血红素对过氧化氢酶产生的影响。过氧化氢酶活性在对数后期达到峰值，而超氧化物歧化酶的比活性在整个培养生长周期中保持恒定。该过氧化氢酶是一种不可透析的、对氰化物和叠氮化物敏感、热不稳定的蛋白质，与牛红细胞过氧化氢酶在琼脂糖6B上共洗脱。对过氧化氢酶活性和血红素染色的聚丙烯酰胺凝胶分析表明，单一催化活性带与三个血红素蛋白带之一相对应。这些数据表明存在一种分子量约为250,000的血红素蛋白。超氧化物歧化酶是一种对氰化物不敏感的蛋白质，分子量约为40,000，在丙烯酰胺凝胶上电泳迁移时表现为单一活性带。
