Abstract
Nutritional interest in the blood aminotransferases is concerned with the in vitro functional evaluation of the relative degree of saturation of total endogenous apoenzyme with vitamin B-6 vitamers, principally pyridoxal-5′-phosphate (PLP). The transamination reactions catalysed by aspartate and alanine aminotransferases (AST and ALT) are outlined in Fig. 1. Both enzymes facilitate the transfer of the amino group from the respective amino acid to 2-oxoglutarate forming L-glutamate and the keto acid corresponding to the original amino acid. Both enzymes are believed to be a mixture (as measured directly by current techniques) of two or more isomers requiring different B-6 vitamers to form the active holoenzyme. A significant portion of the total activity responds to PLP. The ratio of the increase in the endogenous enzyme activity resulting from exogenous adjunct of PLP to the original endogenous activity is used by some as an indicator of vitamin B-6 status.
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Skala, J.H., Waring, P.P., Lyons, M.F., Rusnak, M.G., Alletto, J.S. (1981). Methodology for Determination of Blood Aminotransferases. In: Leklem, J.E., Reynolds, R.D. (eds) Methods in Vitamin B-6 Nutrition. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9901-8_10
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DOI: https://doi.org/10.1007/978-1-4684-9901-8_10
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