Disease relevance of iodoacetamide

• Bacterial endotoxin was administered with iodoacetamide-modified P1798 lymphoma cells to immunize syngenic BALB/cJ mice against this lymphoma to which they are naturally unresponsive [1].
• RESULTS: Iodoacetamide induced a mild gastritis [2].
• Iodoacetate behaves as an affinity label for the Escherichia coli enzyme with a Ki of 30 mM and a limiting inactivation rate of 0.014 min-1 at pH 7.0 and 25 degrees C. Affinity labeling is mediated by the negative charge of the reagent since iodoacetamide does not inactivate the enzyme [3].
• Enzymatically inactive variants of chicken liver fatty acid synthetase have been prepared by specific chemical modification of the active cysteine SH group with iodoacetamide, and the phosphopantetheine SH group with chloroacetyl-CoA [4].
• Male Sprague-Dawley rats were fasted 18 h and given streptozocin (STZ; 60 mg/kg body wt i.p.). The resultant diabetes mellitus, not treated with insulin, was associated with persistent manifoldly increased plasma IgA levels, as measured by single-radial immunodiffusion after reduction with dithiothreitol and alkylation with iodoacetamide [5].

Psychiatry related information on iodoacetamide

• The inhibited gastric motor activity induced by clarithromycin was not modified by pretreatment with either indomethacin or iodoacetamide [6].

High impact information on iodoacetamide

• Monomeric MBP can be isolated from serum by reduction of serum with dithiothreitol, alkylation with iodoacetamide, and acidification to pH 2 followed by fractionation on Sephadex G-50 at pH 2 [7].
• Nodose and T9, T10 dorsal root ganglia were removed 7 days after initiation of iodoacetamide treatment [2].
• Long-term feeding with iodoacetamide also resulted in enhanced gastrin release and antral gastrin messenger RNA in response to a meal supplemented with AmAc, but not to a normal meal or one supplemented with sodium acetate [8].
• Further, substrate (EGFR) and phosphatase have been separated: a membrane preparation of cells that have been treated with epidermal growth factor (EGF) and whose dephosphorylating enzymes have been permanently destroyed by iodoacetamide can be mixed with a membrane preparation from untreated cells which re-establishes EGFR dephosphorylation [9].
• The ability of native PTI to bind thrombin was destroyed by incubation with iodoacetamide [10].

Chemical compound and disease context of iodoacetamide

• DDA was also effective with solubilized tumor antigen and with lymphoma cells not pretreated with IAD, but the latter had to be heat killed to assure that they were nontumorigenic [11].
• However, gastritis induced by iodoacetamide reduced clarithromycin transfer without any effect on metronidazole or amoxicillin transfer [12].
• Human p53 was expressed in E. coli, purified, labeled with fluorescein iodoacetamide (IAF) and characterized for sequence-specific DNA binding and epitope disposition [13].
• The single disulfide bond in Escherichia coli thioredoxin was reduced by reaction with a 20-fold excess of reduced dithiothreitol at neutral pH and 25 degrees C. For some measurements, reduced thioredoxin was further reacted with iodoacetamide to alkylate the cysteinyl residues [14].
• Reduction and alkylation of patient sera with 2-mercaptoethanol and iodoacetamide removed detectable antibody in 78% of the samples, which suggested a dominant role of immunoglobulin M in the response to Bacteroides antigens [15].

Biological context of iodoacetamide

• Rotational correlation time (tau2) were determined for a spin label analog of iodoacetamide bound to the subfragment-1 (S-1) region of myosin under a variety of conditions likely to shed light on the molecular mechanism of muscle contraction [16].
• Platelet activation by sera from 15 patients with TTP was inhibited by leupeptin, iodoacetamide, and antipain but not by phenylmethylsulphonylfluoride, epsilon-aminocaproic acid, soybean trypsin inhibitor, aprotinin, and D-phenylanyl-1-prolyl-1-arginine chloromethyl ketone [17].
• CP activity was independent of both the intrinsic and extrinsic pathways of blood coagulation, using factor IX and factor VII deficient plasmas, and was inhibited by the cysteine proteinase inhibitors iodoacetamide and HgCl2 [18].
• In contrast to the wild type enzyme, inactivation of the mutant proteins was not affected by the presence of the competitive inhibitor phosphate, suggesting that the remaining slow rate of iodoacetamide inactivation is due to modification away from the active site [19].
• The hydrogen exchange kinetics of the N delta H proton in His F8 of iodoacetamide- and N-ethylmaleimide-treated human deoxyhemoglobins were studied using a NMR method [20].

Anatomical context of iodoacetamide

• The ffect of N-ethylmaleimide and iodoacetamide on the glucocorticoid receptor activity extracted from the cytosol of either mouse of hamster cells has been investigated [21].
• Mesophyll protoplasts of Lycopersicon esculentum were treated with iodoacetamide to inactivate mitochondria, and protoplasts of Solanum acaule and Solanum tuberosum were irradiated with gamma- or x-rays to inactivate nuclei [22].
• Proteolysis in the cell-free system and in intact reticulocytes was inhibited by the same agents (L-l-tosylamido-2-phenyl-ethylchloromethyl ketone, N-alpha-p-tosyl-L-lysine chloromethyl ketone, N-ethylmaleimide, iodoacetamide, and o-phenanthroline) [23].
• An increase in the quantity of exposed sulfhydryl groups of normal young and mature rat liver rough endoplasmic reticulum after stripping by ethylenediaminetetraacetate and potassium chloride was observed with iodoacetamide [24].
• Exposed sulfhydryl groups of normal mature female rat liver smooth endoplasmic reticulum were decreased to a similar degree by the stripping procedure with ethylenediaminetetra-acetate and potassium chloride when quantitated by either iodoacetamide or 4,4'-dithiodipyridine [24].

Associations of iodoacetamide with other chemical compounds

• N-Ethylmaleimide (10 mM) and iodoacetamide (1.5 mM) inhibited DNA polymerase-alpha activity completely, whereas only 35-40% inhibition was observed for DNA polymerase-beta under similar conditions [25].
• Both enzymes were inactivated by reaction with iodoacetamide; however, addition of the substrate, formate, was necessary to render the enzymes susceptible to alkylation [26].
• Inactivation of the enzyme by alkylation with iodoacetamide indicated that at least 1 cysteine residue in the protein is essential for enzyme activity [27].
• Differential labeling of the cysteine residues by iodoacetic acid and iodoacetamide has been followed by electrospray ionization mass spectrometry and positions of the labels determined by analysis of tryptic fragments [28].
• Alkylation of the protein with excess iodoacetamide also led to inactivation, although titration with 5,5'-dithiobis-(2-nitrobenzoic acid) indicated that the protein initially contained no free sulfhydryl moieties [29].

Gene context of iodoacetamide

• Preincubation with iodoacetamide prevented the formation of the two high-molecular-weight complexes without affecting noncovalent dimer formation or high-affinity IL-3 binding [30].
• Grx1 and Grx2 were sensitive to inactivation by iodoacetamide and H(2)O(2) and exhibited similar pH dependence of catalytic activity [31].
• In contrast with iodoacetamide-treated red cells, catalase was not inactivated by 3-AT in glutathione peroxidase-deficient erythrocytes [32].
• Defensin interactions with either alpha 1-PI or alpha 1-ACT were not affected by iodoacetamide or high salt concentration [33].
• Using an iodoacetamide derivative of the Eu3+-chelate of N-(p-benzoic acid)diethylenetriamine-N,N',N"-tetraacetic acid (DTTA), incorporation of one Eu3+ per IL8 molecule ([Eu3+]IL8-S72C) was achieved [34].

Analytical, diagnostic and therapeutic context of iodoacetamide

• Sequence alignment indicates that the reactive center P1 residue is Cys-344, consistent with abrogation of elastase inhibitory activity by iodoacetamide and making EI a naturally occurring Cys-serpin [35].
• The pKa values obtained by titration of mutant proteins with iodoacetamide at different pHs were 5.0 for Cys-60 and 8.2 for Cys-117 [36].
• Similar effects were detected after treatment of the enzyme with iodoacetamide [37].
• The b chain in which one disulfide bond is reduced and in which the two sulfhydryl groups formed are alkylated with iodoacetamide binds with a2 zymogen to give a complex that is indistinguishable by exclusion chromatography from plasma zymogen [38].
• The identification of transglutaminase in the growth-factor-dependent mouse mast cell line PT18 was accomplished through its characteristic catalytic properties (specificity, calcium dependency, and inhibition by iodoacetamide); and by both immunoprecipitation and Western blot analysis using affinity purified antibody [39].

References