Low I E, Eaton M D, Proctor P
J Bacteriol. 1968 Apr;95(4):1425-30. doi: 10.1128/jb.95.4.1425-1430.1968.
No catalase activity was detected in four strains of glucose-grown Mycoplasma pneumoniae at any time during the replication of the organism. Exogenous catalase dramatically increased the O(2) uptake with glycerol, presumably by releasing inhibition caused by hydrogen peroxide. The effect of added catalase on the O(2) uptake of washed organisms with glucose as substrate was moderate and variable in degree. The production of hydrogen peroxide was demonstrated by the quantitative enzymatic assay for inorganic peroxide and by the fact that added pyruvate, which is non-enzymatically oxidized by H(2)O(2) to acetic acid and CO(2) could mimic the action of catalase.
在以葡萄糖培养的四株肺炎支原体中,在该生物体复制的任何阶段均未检测到过氧化氢酶活性。外源性过氧化氢酶显著增加了甘油的氧气摄取量,推测这是通过解除过氧化氢引起的抑制作用实现的。添加的过氧化氢酶对以葡萄糖为底物的洗涤后生物体的氧气摄取量的影响适中且程度不一。通过对无机过氧化物的定量酶促测定以及添加的丙酮酸(丙酮酸可被过氧化氢非酶氧化为乙酸和二氧化碳)能够模拟过氧化氢酶的作用这一事实,证明了过氧化氢的产生。