2-Iodosobenzoic acid (IBA) may be used to study enzyme structure and activity. IBA is used as an oxidant which oxidizes vicinal sulfhydryls to disulfides (cysteine residues) within enzymes leading to their inactivation or conformational changes. IBA is also used to cleave tryptophanyl peptide bonds.
Biochemical and biophysical research communications, 168(2), 659-664 (1990-04-30)
The active form of protein B2, the small subunit of ribonucleotide reductase from E. Coli, contains a binuclear non heme iron center and a tyrosyl radical. MetB2 is an inactive form that lacks the radical but retains the Fe(III) center.
A series of soluble and insoluble polymer supported versions of the versatile oxidizing reagent IBX has been prepared. Each of the reagents were evaluated for their efficiency in the conversion of benzyl alcohol to benzaldehyde. Results from this study were
The Journal of biological chemistry, 266(4), 2652-2659 (1991-02-05)
When the enzymatically active A-fragment of diphtheria toxin is translocated to the cytosol, the B-fragment inserts into the membrane in such a way that a 25-kDa polypeptide becomes shielded from proteases added to the external medium. We have attempted to
The International journal of biochemistry, 21(5), 549-554 (1989-01-01)
1. Tryptic cleavage sites in bovine secretory component (SC) which become inaccessible when SC is bound to IgA dimer remained inaccessible at 60 degrees C and in 4 M urea at 37 degrees C. 2. This suggests the presence of
The amino acid sequence of the neutral zinc protease from Bacillus mesentericus strain 76 (MCP 76) has been determined by using peptides derived from digests with trypsin, chymotrypsin, and cyanogen bromide and from cleavage with o-iodosobenzoic acid. The peptides were
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