Journal article

Publication year: 1997

Pages: 318-320

Journal: FEBS Letters

Volume number: 412

Issue number: 2

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/S0014-5793(97)00816-8

Publisher: Wiley

Abstract: 
The flavoprotein thioredoxin reductase [EC 1.6.4.5] NADPH+H+ + thioredoxin-S-2 --> NADP(+) + thioredoxin-(SH)(2)) was isolated from mouse Ehrlich ascites tumour (EAT) cells, Like the counterpart from human placenta but unlike the known thioredoxin reductases from non-vertebrate organisms, the mouse enzyme has found to contain 1 equivalent of selenium per subunit of 58 kDa, The K-M values were 4.5 mu M for NADPH, 480 mu M for DTNB and 36 mu M for Escherichia coli thioredoxin, the turnover number with DTNB being approximate to 40 s(-1). As mouse is a standard animal model in cancer and malaria research, thioredoxin reductase and glutathione reductase [EC 1.6.4.2] from EAT cells, were compared with each other, While both enzymes in their 2-electron reduced form are targets of the cytostatic drug carmustine (BCNU), no immunologic cross-reactivity between the two mouse disulfide reductases was observed. (C) 1997 Federation of European Biochemical Societies.

Harvard Citation style: Gromer, S., Schirmer, R. and Becker, K. (1997) The 58 kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase, FEBS Letters, 412(2), pp. 318-320. https://doi.org/10.1016/S0014-5793(97)00816-8

APA Citation style: Gromer, S., Schirmer, R., & Becker, K. (1997). The 58 kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase. FEBS Letters. 412(2), 318-320. https://doi.org/10.1016/S0014-5793(97)00816-8