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. Safety of 2-Iodoacetamide.
Mamo, Jermen;Kangwa, Martin;Suarez Orellana, Jorge Fernando;Yelemane, Vikas;Fernandez-Lahore, Hector Marcelo;Assefa, Fassil research published 《 Purification and Characterization of Aspartic Protease Produced from Aspergillus oryzae DRDFS13 MN726447 under Solid-State Fermentation》, the research content is summarized as follows. Aspartic proteases (E.C.3.4.23.) are endopeptidases with mol. masses ranging between 30-45 kDa. They depend on aspartic acid residues for their catalytic activity and show maximal activity at low pH. Thus the main objective of the present study was to purify and characterize aspartic protease from locally identified fungi. The aspartic protease in the current study was obtained from A. oryzae DRDFS13 under SSF (solid-state fermentation). The crude enzyme extract was purified by size-exclusion (SEC) and ion-exchange (IEC) chromatog. The milk-clotting activity (MCA), protease activity (PA); the presence of N-glycosylation, inhibition studies and mol. weight were determined using standard methods. Optimum temperature and stability, optimum pH and stability on MCA were assessed using standard methods. The highest MCA (477.11 U/mL), specific activity (183.50 U/mg), purification fold (6.20) and yield (9.2%) were obtained from IEC fraction A8. The mol. weight of 40 kDa was assigned for IEC A8.The protein was glycosylated. Incubation of the IEC A8 with pepstatin A caused a 94% inhibition on MCA. The enzyme showed maximum MCA at 60°C and pH 5.0 with stability at pH 4.5-6.5 and temperature 35-45°C. Furthermore, the results obtained in the present study confirmed that the aspartic protease enzyme produced from A. oryzae DRDFS13 could be used as a substitute source of rennet enzyme for cheese production
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., Safety of 2-Iodoacetamide
Referemce:
Iodide – Wikipedia,
Iodide – an overview | ScienceDirect Topics – ScienceDirect.com