Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi

被引：9

作者：

Favaloro, B

Melino, S

Petruzzelli, R

Di Ilio, C

Rotilio, D

机构：

[1] Ist Ric Farmacol Mario Negri, Consorzio Mario Negri Sud, Gennaro Paone Environm Hlth Ctr, I-66030 Santa Maria Imbaro, Italy

[2] Univ G dAnnunzio, Fac Med, Dipartimento Sci Biomed, Chieti, Italy

来源：

FEMS MICROBIOLOGY LETTERS | 1998年 / 160卷 / 01期

关键词：

glutathione transferase; Ochrobactrum anthropi; N-terminal sequence;

D O I：

10.1016/S0378-1097(98)00015-9

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Glutathione transferase was purified from Ochrobactrum anthropi and its N-terminal sequence was determined to be MKLYYKVGACSLAPHIILSEAGLPY. The apparent molecular mass of the protein (24 kDa) was determined by SDS-polyacrylamide gel electrophoresis analysis. The amino acid sequence obtained showed similarities with known bacterial glutathione transferases in the range of 72-64%. Immunoblotting experiments performed with antisera raised against glutathione transferase from O. anthropi did not show cross-reactivity with two bacterial glutathione transferases belonging to Serratia marcescens and Proteus mirabilis. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.

引用

页码：81 / 86

页数：6

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