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 Microbioljournal_title
Letters in applied microbiologyauthors
García-Ortega L,Lacadena J,Lacadena V,Masip M,De Antonio C,Martínez-Ruiz A,Martínez Del Pozo Adoi
10.1046/j.1472-765x.2000.00714.xsubject
Has Abstractpub_date
2000-04-01 00:00:00pages
298-302issue
4eissn
0266-8254issn
1472-765Xpii
lam714journal_volume
30pub_type
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