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.
A previously developed model of exercise-induced muscle contracture using iodoacetate to inhibit glyceraldehyde-3-phosphate dehydrogenase in rat hindlimb muscles produced selective type II myofiber damage. Utilizing a modification of the same model system, rats were given intra-aortic ortho-iodosobenzoic acid (700 nmol/kg
Developing potent detoxification strategies for prophylaxis and therapy against organophosphate (OP) intoxication still represents a challenging task. Clinical application of numerous investigated substances including enzymes and low molecular scavengers like metal ions or nucleophiles could not yet be realised due
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
Archives of biochemistry and biophysics, 360(2), 187-194 (1998-12-16)
Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was inactivated by peroxynitrite under biologically relevant conditions. The decrease of enzymatic activity followed an exponential function, and the concentration of peroxynitrite needed to inactivate 50% of 7 microM GAPDH (IC50) was 17 microM. Hydroxyl
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