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Arginine was first isolated from lupin seedlings in 1886 and was thereafter identified as a component of animal proteins. Arginase, the enzyme that hydrolyzes arginine to ornithine and urea was identified in liver in 1904. Later, the discovery of the urea cycle by Krebs and Henseleit in 1932 elucidated the role of arginine in physiology and metabolic pathway.1 The dietary essentiality of arginine was discovered in 1950 when Rose found that young growing rats demonstrated more rapid growth when receiving dietary arginine. The role of arginine in wound healing was demonstrated first in animals placed on an arginine-deficient diet. Arginine supplementation has been shown to enhance collagen synthesis and wound strength. Rats fed an arginine-deficient diet after minor trauma had increased postoperative weight loss and increased mortality when compared with rats fed a similar defined diet containing arginine. Though several pathways have been studied, the exact mechanism of action of arginine on wound healing and collagen metabolism is not known.

Arginine, a dibasic amino acid, is considered to be a dietary conditionally dispensible amino acid. Arginine is synthesized endogenously in the kidney from gut-derived citrulline. The small intestine converts dietary amino acids to citrulline. The quantities of arginine produced normally are sufficient to maintain muscle and connective tissue mass. However, endogenous synthesis of arginine is insufficient to meet the heightened demands that increased protein turnover requires during period of stress.

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