PMID: 2500149Jul 7, 1989Paper

Expression of human erythrocyte NADH-cytochrome b5 reductase as an alpha-thrombin-cleavable fused protein in Escherichia coli

Biochimica Et Biophysica Acta
K ShirabeM Takeshita

Abstract

Recombinant fused protein containing human erythrocyte NADH-cytochrome b5 reductase (cytochrome b5 reductase, EC 1.6.2.2.) was produced in Escherichia coli, which was linked to the NH2 terminus of beta-galactosidase of the vector pUC13 via a recognition sequence of alpha-thrombin. Cleavage of purified fused protein with alpha-thrombin yielded the enzyme whose apparent molecular weight (32,000) was the same as the native enzyme. The amino-acid sequence from Phe-1 to Leu-10 was determined to be identical to that of the authentic enzyme. The purified enzyme showed an identical absorption spectrum and similar catalytic properties to the native enzyme. Establishment of the expression system would make it possible to determine the reaction mechanism of the enzyme.

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Citations

Jun 25, 2003·Protein Expression and Purification·C Ainsley Davis, Michael J Barber
Apr 3, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Sangwoo KimTomitake Tsukihara
Jan 16, 2007·The FEBS Journal·Carole L Linster, Emile Van Schaftingen
Jul 4, 2006·Archives of Biochemistry and Biophysics·Glenn W RomaMichael J Barber
Nov 2, 2012·Critical Reviews in Biotechnology·Fatemeh ElahianSeyed Abbas Mirzaei
Oct 26, 2001·Protein Expression and Purification·M J Barber, G B Quinn
Aug 14, 2012·Environmental Toxicology and Pharmacology·Zai-Yong WangZheng-Tao Wang
Feb 7, 2014·The Journal of Biological Chemistry·Courtney E Sparacino-WatkinsMark T Gladwin
Jun 1, 1995·Journal of Bioenergetics and Biomembranes·B DurhamA Willie
Aug 1, 1990·Trends in Biochemical Sciences·W H Campbell, K R Kinghorn
May 1, 1992·Archives of Biochemistry and Biophysics·M E Brandt, L E Vickery

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