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.
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
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, 269(10), 7290-7296 (1994-03-11)
The calmodulin binding domain of the type I adenylyl cyclase has recently been identified as an amino acid sequence (residues 495-522) that contains 2 cysteine residues. Therefore, we examined the effect of several sulfhydryl reagents on the calmodulin sensitivity of
Bovine retinal S-antigen was cleaved by three chemical cleavage procedures including o-iodosobenzoic acid (IBA), mile acid and cyanogen bromide. The resultant peptides were used to study antibody-defined epitopes. Treatment with IBA, which cleaves primarily at tryptophanyl peptide bonds, produced at
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