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Reduction of biological activity of murine recombinant interleukin‐1β by selective deamidation at asparagine‐149
Author(s) -
Gaston O. Daumy,
Cheryl Wilder,
Joseph M. Merenda,
Alexander S. McColl,
Kieran F. Geoghegan,
Ivan G. Otterness
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)80093-i
Subject(s) - deamidation , recombinant dna , asparagine , chemistry , biological activity , escherichia coli , beta (programming language) , biochemistry , tris , stereochemistry , amino acid , in vitro , enzyme , gene , computer science , programming language
A biologically active preparation of murine recombinant interleukin‐1β (mIL‐1β) from Escherichia coli cell lysates contained two forms of mIL‐1β with pI 8.7 and pI 8.1, respectively. Treatment with 0.1 M Tris, pH 8.5, at 37°C for 35 h converted the pI 8.7 form to the pI 8.1 form by the selective deamidation of an asparagine residue (Asn 149 ) in the mIL‐1β molecule. Deamidated mIL‐1β had 3‐ to 5‐fold lower co‐mitogenic activity and receptor affinity than the unmodified form.