Loewen P C, Triggs B L
J Bacteriol. 1984 Nov;160(2):668-75. doi: 10.1128/jb.160.2.668-675.1984.
A class of catalase-deficient mutants that was unlinked to katE was localized between mutS and cys at 59.0 min on the Escherichia coli genome. This locus was named katF. Transposon Tn10 insertions were isolated that mapped in both katE and katF loci. The catalase species present in katE+ and katF+ recombinants was found to be different from the main catalase activities, HPI and HPII, in several respects. It did not have an associated peroxidase activity; it was electrophoretically slower on native polyacrylamide gels; it eluted from DEAE-Sephadex A50 at a higher salt concentration; its Km for H2O2 was 30.9 mM as compared with 3.7 mM for HPI and HPII; its synthesis was not induced by ascorbate; and it did not cross react with HPI-HPII antisera. This new catalase was labeled HPIII.
一类与katE不连锁的过氧化氢酶缺陷型突变体定位于大肠杆菌基因组59.0分钟处的mutS和cys之间。该位点被命名为katF。分离到了插入在katE和katF位点的转座子Tn10插入突变体。发现katE⁺和katF⁺重组体中存在的过氧化氢酶种类在几个方面与主要的过氧化氢酶活性HPI和HPII不同。它没有相关的过氧化物酶活性;在天然聚丙烯酰胺凝胶上电泳迁移较慢;从DEAE-葡聚糖A50上洗脱时所需盐浓度较高;其对H₂O₂的Km为30.9 mM,而HPI和HPII为3.7 mM;其合成不受抗坏血酸诱导;并且它与HPI-HPII抗血清不发生交叉反应。这种新的过氧化氢酶被标记为HPIII。