Cho Y H, Roe J H
Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University, Korea.
J Bacteriol. 1997 Jun;179(12):4049-52. doi: 10.1128/jb.179.12.4049-4052.1997.
We isolated the catA gene for the major vegetative catalase from Streptomyces coelicolor Müller. It encodes a polypeptide of 488 residues (55,440 Da) that is highly homologous to typical monofunctional catalases. We investigated catA expression by analyzing both catA mRNA and catalase activity. catA expression was increased by H2O2 treatment but did not increase during stationary phase. A putative catalase (CatB) cross-reactive with anti-CatA antibody appeared during stationary phase and in the aerial mycelium.
我们从天蓝色链霉菌Müller中分离出了主要营养过氧化氢酶的catA基因。它编码一个由488个氨基酸残基组成的多肽(55,440道尔顿),与典型的单功能过氧化氢酶高度同源。我们通过分析catA mRNA和过氧化氢酶活性来研究catA的表达。经H2O2处理后,catA的表达增加,但在稳定期并未增加。在稳定期和气生菌丝中出现了一种与抗CatA抗体发生交叉反应的假定过氧化氢酶(CatB)。