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Characterization of a recombinant murine interleukin-6: assignment of disulfide bonds.

Abstract：

:Murine interleukin 6 (mIL-6) has been synthesized as a fusion protein using a lac operon inducible plasmid in Escherichia coli. The first 8 amino acids are from the N-terminus of bacterial beta-galactosidase and the last 175 amino acids are from residue number 12 to the end of native mIL-6. This fusion protein is equipotent with the native molecule in the hybridoma growth factor assay and has comparable receptor binding characteristics. The two disulfide bridges in mIL-6 have been identified by Staphylococcus aureus V8 protease peptide mapping and Edman degradation of cystine-containing peptides. It has been shown that there are disulfide bonds between Cys46-Cys52 and Cys75-Cys85.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Simpson RJ,Moritz RL,Van Roost,Van Snick J

doi

10.1016/s0006-291x(88)80056-1

subject

Has Abstract

pub_date

1988-11-30 00:00:00

pages

364-72

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80056-1

journal_volume

157

pub_type

杂志文章

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