Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. Formula: C2H4INO.
Mukherjee, Abhishek research published 《 Purification, characterisation and immobilisation of an acid-stable, raw-starch hydrolysing thiol β-amylase, over produced in the stem of Paederia foetida》, the research content is summarized as follows. A 200-kDa acid-stable thiol β-amylase, appreciably present in the stem of Paederia foetida (48,000 ± 5,500 Units (U)/100 g fresh weight) was purified by (NH4)2SO4 precipitation, ion exchange chromatog., size exclusion chromatog. and HPLC. The enzyme was optimally active in pH 6.0 at 60°, showed a specific activity of 3466 U/mg protein and displayed a Km of 3.5 ± 0.1 mg/mL (soluble starch). Activity was stable in the pH range of 3.0-8.0, retaining 94 ± 1% activity at pH 3. The enzyme was stable up to 55-57°, beyond which the activity fell sharply. Hg2+ and Ag+ (1 mM concentration) completely inhibited the enzyme activity. Enzyme was strongly inhibited by DTNB, PCMB, N-ethylmaleimide, iodoacetic acid, iodoacetamide, and was exptl. determined to be a thiol amylase (3 SH group/mol); the DTNB inhibition of activity being released by cysteine. The enzyme efficiently hydrolyzed potato starch (DE = 51), corn starch (DE= 46), gelatinised cereal flours (wheat, rice and gram), amylopectin, raw starch and raw cereal flours. The enzyme was determined to be a β-amylase (maltose as the only product) by end product anal. and its inability to hydrolyze β-limit dextrin. Immobilization of the enzyme (crude) on oxidized bagasse (dialdehyde cellulose) increased the temperature optima (by 10°) and thermo-stability (retaining 48 ± 2% and 38 ± 1% activity at 70° and 80°, resp.). The immobilized enzyme system efficiently produced maltose from cereal and tuber starches, remaining 85 ± 1% and 80 ± 1% active after the tenth and twentieth cycles, resp.
144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.
2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., Formula: C2H4INO
Referemce:
Iodide – Wikipedia,
Iodide – an overview | ScienceDirect Topics – ScienceDirect.com