Thioglycolic acid corresponding disulfide (2-[(carboxymethyl)disulfanyl]acetic acid or dithiodiglycolic acid): Thioglycolic acid, usually as its dianion, forms complexes with metal ions. Such complexes have been used for the detection of iron, molybdenum, silver, and tin. Thioglycolic acid reacts with diethyl acetylmalonate to form acetylmercaptoacetic acid and diethyl malonate, the reducing agent in conversion of Fe(III) to Fe(II). Scientist David R. Goddard, in the early 1930s, identified TGA as a useful reagent for reducing the disulfide bonds in proteins, including keratin (hair protein), while studying why protease enzymes could not easily digest hair, nails, feathers, and such. He realized that while the disulfide bonds,
Protein phosphatase Protein phosphatase A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for