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Detection of a novel catalase in extracts of Mycobacterium avium and Mycobacterium intracellulare.

机译:检测鸟分枝杆菌和胞内分枝杆菌提取物中的新型过氧化氢酶。

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A novel class of catalase, which differs from the previously described M- and T-catalases of mycobacteria, was detected in strains of Mycobacterium avium and M. intracellulare. Designated A-catalase, this enzyme resisted inactivation at 68 degrees C, was inactivated by 3-amino-1,2,4-triazole (aminotriazole), and exhibited no peroxidase activity. All of these properties distinguished the enzyme from T-catalase. The A-catalase exhibited a Km of 70 mM H2O2, which is between the upper and lower extremes of the ranges reported for T- and M-catalases, respectively. The A-catalase appeared to be more hydrophobic than M-catalase and did not react with antiserum to a representative sample of this class. The banding patterns of T- and M-catalases seen by polyacrylamide gel electrophoresis (PAGE) were essentially unaffected by the incorporation of sodium dodecyl sulfate (SDS) into the PAGE system, whereas the single band of A-catalase seen by PAGE without SDS resolved into as many as five bands in the presence of SDS; these bands were all of slower mobility than the original band. The banding pattern seen with SDS appeared to be related more to counterion charge effects than to molecular size increases that could be attributed to SDS complexed to the protein. It remains to be determined whether the multiple A-catalase bands reflect different proteins or different SDS micellar complexes of a single protein.
机译:在鸟分枝杆菌和胞内分枝杆菌菌株中检​​测到一类新型的过氧化氢酶,该酶与以前描述的分枝杆菌的M-和T-催化不同。被指定为A-过氧化氢酶,该酶在68℃下抵抗失活,被3-氨基-1,2,4-三唑(氨基三唑)灭活,并且没有过氧化物酶活性。所有这些特性使酶与T-过氧化氢酶区分开。 A-过氧化氢酶的Km为70 mM H2O2,分别介于T-和M-催化的范围的上限和下限之间。 A-过氧化氢酶似乎比M-过氧化氢酶更具疏水性,并且与此类代表性样品的抗血清没有反应。聚丙烯酰胺凝胶电泳(PAGE)观察到的T-和M-催化的条带模式基本上不受十二烷基硫酸钠(SDS)加入PAGE系统的影响,而PAGE观察到的A-过氧化氢酶的单条带却没有分离在存在SDS的情况下可分为多达五个频段;这些频段的移动性都比原始频段慢。用SDS观察到的条带模式似乎更多地与抗衡离子电荷效应有关,而不是与分子大小增加有关,后者可能归因于SDS与蛋白质复合。多个A-过氧化氢酶带是否反映不同的蛋白质或单个蛋白质的不同的SDS胶束复合物尚待确定。

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