Di Ilio C, Aceto A, Allocati N, Piccolomini R, Bucciarelli T, Dragani B, Faraone A, Sacchetta P, Petruzzelli R, Federici G
Istituti di Scienze Biochimiche, Facoltà di Medicina, Università di Chieti, Italy.
Arch Biochem Biophys. 1993 Aug 15;305(1):110-4. doi: 10.1006/abbi.1993.1399.
A single form of glutathione transferase (Xc-GST-4.5) having an isoelectric point at pH 4.5 was resolved from Xanthomonas campestris cytosol by affinity chromatography and isoelectric focusing. HPLC,N-terminal amino acid sequence, and SDS-PAGE analyses indicate that Xc-GST-4.5 is composed of two identical subunits, each with a molecular mass of 22 kDa. As indicated by its substrate specificity, immunological reactivity, and CD spectra, as well as by its N-terminal amino acid sequence, Xc-GST-4.5 appears to be distinct from the other bacterial glutathione transferases, Pm-GST-6.0 and Sm-GST-7.3, previously purified from the cytosolic fraction of Proteus mirabilis and Serratia marcescens. Xc-GST-4.5 also appears to be distinct from the GST so far purified from other sources.
通过亲和色谱和等电聚焦从野油菜黄单胞菌胞质溶胶中分离出一种单一形式的谷胱甘肽转移酶（Xc-GST-4.5），其等电点为pH 4.5。高效液相色谱、N端氨基酸序列和SDS-PAGE分析表明，Xc-GST-4.5由两个相同的亚基组成，每个亚基的分子量为22 kDa。从其底物特异性、免疫反应性、圆二色光谱以及N端氨基酸序列来看，Xc-GST-4.5似乎与先前从奇异变形杆菌和粘质沙雷氏菌胞质部分纯化得到的其他细菌谷胱甘肽转移酶Pm-GST-6.0和Sm-GST-7.3不同。Xc-GST-4.5似乎也与目前从其他来源纯化得到的谷胱甘肽转移酶不同。
