The solubility of the ribotoxin alpha-sarcin, produced as a recombinant protein in Escherichia coli, is increased in the presence of thioredoxin.

Abstract:

:The yield of purified recombinant alpha-sarcin increases approximately three- to fourfold when this toxin is co-expressed in Escherichia coli with thioredoxin. This increased production is attributed to the existence, in the presence of thioredoxin, of a reducing environment which allows rearrangement of incorrect disulphide bonds to produce the soluble native conformation. The protein thus produced retains the structural, spectroscopic and enzymatic features of the natural fungal alpha-sarcin.

journal_name

Lett Appl Microbiol

authors

García-Ortega L,Lacadena J,Lacadena V,Masip M,De Antonio C,Martínez-Ruiz A,Martínez Del Pozo A

doi

10.1046/j.1472-765x.2000.00714.x

subject

Has Abstract

pub_date

2000-04-01 00:00:00

pages

298-302

issue

4

eissn

0266-8254

issn

1472-765X

pii

lam714

journal_volume

30

pub_type

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