Disease relevance of o-Iodosobenzoate

• Overlapping peptides were obtained by cleavage with o-iodosobenzoic acid, or digestion with Staphylococcus aureus protease, thermolysin and pepsin [1].
• Transport of beta-globin mRNA from nuclei of murine Friend erythroleukemia cells. Reversible inhibition of transport by the oxidizing sulfhydryl reagent o-iodosobenzoate [2].

High impact information on o-Iodosobenzoate

• Further cleavage of this peptide with o-iodosobenzoic acid at a tryptophanyl peptide bond revealed that an Mr 5,000 peptide (with the amino-terminal sequence Trp-Phe-Thr-Cys-Val-Leu) bound to a high Mr kininogen affinity column and inhibited binding of 125I-factor XI to high Mr kininogen [3].
• 4-Aminobutyrate aminotransferase is inactivated by preincubation with iodosobenzoate at pH 7 [4].
• Sulfhydryl residues exposed during activation can be reoxidized to disulfide by incubation with iodosobenzoate , with a concomitant loss of ATPase activity [5].
• The approximate positions of the IBA peptides in the VP1 sequence were determined by cleavage of formic acid fragments with IBA [6].
• Amino acid sequence analyses were carried out on V8 protease, CNBr, and iodosobenzoic acid digestion fragments [7].

Biological context of o-Iodosobenzoate

• Menadione and o-iodosobenzoic acid inhibited nitroreductase activity in all of the isolates, indicating the involvement of sulfhydryl groups in the active site of the enzyme [8].
• Thiol oxidants, iodosobenzoic acid or diamide, reverted the effects of DTTred on psbA gene expression [9].
• Micellar solutions of CTAB have been found to accelerate the hydrolysis of alpha-naphthyl acetate (alpha-NA) by o-iodosobenzoic acid (IBA), a strong nucleophile [10].
• 6. The product formation kinetics of acid phosphatase, beta-amylase and NADPH2 cytochrome-c reductase in the absence and in the presence of inhibitors, mercuric acetate and o-iodosobenzoate is described [11].
• 2. Modification of chloroplasts in the light with o-iodosobenzoate resulted in the inhibition of photophosphorylation and ATPase [12].

Anatomical context of o-Iodosobenzoate

• Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments [13].

Associations of o-Iodosobenzoate with other chemical compounds

• The number of peptides produced, their respective sizes, and their order in the intact VP1 molecule agree with predictions made from available sequence data, both for formic acid cleavage and IBA cleavage [6].
• Cleavage at the two tryptophan residues with o-iodosobenzoic acid was also used to isolate fragments suitable for amino acid sequence analysis [14].
• The amino acid sequence of human factor D is proposed from the analysis of the peptides produced by treatment of the factor D with cyanogen bromide, iodosobenzoic acid, trypsin and V-8 protease [15].
• The reagents 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB), iodosobenzoate, and ethylenimine were able to decrease amiloride-inhibited sodium uptake into vesicles when used at low concentrations [16].
• Treatment of recombinant ER DNA-binding domain (ER-DBD) or ER-enriched extracts from CHO(ER) and MCF-7 cells with thiol-reacting oxidants (diamide, iodosobenzoate, H2O2) or alkylator (iodoacetamide) produces a dose-dependent loss in ER DNA-binding capacity [17].

Gene context of o-Iodosobenzoate

• The C-terminal part of ligand filled porcine estradiol receptor extending from H267 to I595 was isolated by adsorption to the monoclonal antibody 13H2, subjected to cleavage by CNBr, o-iodosobenzoic acid and endopeptidase Lys-C as well as other proteases, both in the native and the denatured state [18].
• 2. Amino acid sequence of the S-loop of the regions of GAPDH from carp muscle was established through the analysis of tryptic digests of the enzyme treated alternatively with bromocyanate and o-iodosobenzoic acid [19].
• Altogether, these observations are consistent with the concept that inactivation of 4-aminobutyrate aminotransferase by iodosobenzoate proceeds through disulfide bond formation between vicinal cysteinyl residues of the protein [20].
• The intact protein was also cleaved with lysyl endopeptidase and o-iodosobenzoic acid [21].
• The amino acid sequence was determined by automated Edman degradation of fragments obtained from degradation with CNBr and iodosobenzoic acid as well as by digestion with Glu-C endopeptidase of reduced and alkylated M-CSF [22].

Analytical, diagnostic and therapeutic context of o-Iodosobenzoate

• Immunoprecipitation of specifically labeled peptide fragments after digestion of photoaffinity-labeled FLAP by iodosobenzoic acid at 72Trp demonstrates that the inhibitors bind to FLAP amino-terminal to this residue [23].
• Following cleavage of the tiger shark light chain with o-iodosobenzoic acid which cleaves at tryptophanyl residues, a constant region peptide was isolated by gel filtration [24].

References