Abstract
l-arginine (2-amino-5-guanidinovaleric) was isolated in 1886 from lupin seedlings. Nine years later, it was also found in animal tissues. Examinations into its function and biochemical structure started in the 1930s. Since then, l-arginine has been described to be involved in numerous biochemical pathways and metabolic processes. For example, in the liver, arginine plays a role in the urea cycle for the removal of ammonia from the body. It is also a substrate for the biological synthesis of creatine (a precursor of creatinine) [Wys and Kaddurah-Daouk (Physiol Rev 80:1107–1113, 2000)]. Although it can be synthesised endogenously, there are some conditions in which arginine cannot be synthesised adequately to meet metabolic demands, such as a consequence of physical injuries or renal insufficiency [Flynn et al. (Biomed Pharmather 56:427–438, 2002)]. In other words, it can act as a conditionally essential amino acid.
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Pedrycz, A., Preedy, V.R. (2017). l-Arginine and the Expression of HSP70 and p53 Proteins. In: Patel, V., Preedy, V., Rajendram, R. (eds) L-Arginine in Clinical Nutrition. Nutrition and Health. Humana Press, Cham. https://doi.org/10.1007/978-3-319-26009-9_2
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DOI: https://doi.org/10.1007/978-3-319-26009-9_2
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