Chain cleaving agents

In a given protein inaccessibility of tryptophan units to NBS may not necessarily mean stability to enzymatic cleavage. In TMV-protein, for instance, all three tryptophan peptide bonds are cleaved by the action of chymotrypsin. This means that the approach of a chemical cleaving agent and of an enzjnne is affected by the same enviromental factors to a different degree. Exclusive iodination of the A chain of insulin is a related example of an unreactive tyrosine residue in the B chain (Springell, 1961). 

Athey, Mosher and Weston (19. 20) studied the use of S3ra net-rical difunctional chain transfer agents for synthesis of tele-chelic polymers. Dithiodiglycolic acid (DTDGA, II) was selected in the present work as a chain transfer agent to Increase the functionality of the PnBA. This particular chain transfer agent cleaves at the sulphur-sulphur bond in the presence of a free radical as shown below ... 

Lysozyme is an enzyme that hydrolyzes polysaccharide chains. It ruptures certain bacterial cells by cleaving the polysaccharide chains that make up their cell wall. Lysozyme is found in many body fluids, but the most thoroughly studied form is from hen egg whites. The Russian scientist P. Laschtchenko first described the bacteriolytic properties of hen egg white lysozyme in 1909. In 1922, Alexander Fleming, the London bacteriologist who later discovered penicillin, gave the name lysozyme to the agent in mucus and tears that destroyed certain bacteria, because it was an enzyme that caused bacterial lysis. 

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