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Human interleukin‐5 expressed in Escherichia coli : assignment of the disulfide bridges of the purified unglycosylated protein
Author(s) -
Proudfoot Amanda E.I.,
Davies J.Gwynfor,
Turcatti Gerardo,
Wingfield Paul T.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80553-f
Subject(s) - escherichia coli , disulfide bond , chemistry , enterobacteriaceae , biochemistry , microbiology and biotechnology , biology , gene
Human interleukin‐5 is a homodimer: each subunit contains two cysteine residues that form two inter‐subunit disulfide bonds. The topology of the disulfides in recombinant human interleukin‐5 produced in Escherichia coli was studied by proteolytic digestion and peptide mapping. Disulfide linked peptides containing cysteine 42 linked to cysteine 84 were isolated. This indicated that cysteine 42 and 84 of one subunit were linked in an antiparallel manner to cysteines 84 and 42 of the other subunit.