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Dietary tryptophan level and the enzymes of tryptophan NAD pathway

Published online by Cambridge University Press:  25 February 2008

U. Satyanarayana  and
B. S. Narasinga Rao
U. Satyanarayana
Affiliation:
National Institute of Nutrition, Indian Council of Medical Research, Jamai Osmania (P.O.), Hyderabad-500 007, India
B. S. Narasinga Rao
Affiliation:
National Institute of Nutrition, Indian Council of Medical Research, Jamai Osmania (P.O.), Hyderabad-500 007, India
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Abstract

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1. Dietary tryptophan was found to regulate the activities of tryptophan oxygenase (EC I. 13.I. 12)and quinolinate phosphoribosyltransferase (EC z.4. 2a) in liver.

2. With increasing tryptophan concentration in the diet containing 100 g protein/kg, tryptophan oxygenase activity increased while that of quinolinate phosphoribosyltransferase decreased. The response of these enzymes to dietary tryptophan at lower dietary protein level (25 g/kg) was not significant.

3. Liver nicotinate phosphoribosyltransferase (EC 2.4.2. 11)activity and kidney picolinate carboxylase (EC 4. I.I. 45) activity were unaltered with different tryptophan concentrations in the diet.

4. The response of various biochemical measurements was dependent on the tryptophan intake and the changes were marked below and above the requirement level of tryptophan.

5. It is suggested that the urinary excretion of quinolinic acid and N'-methylnicotinamide may be useful in assessing the tryptophan nutritional status and its requirement.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 43 , Issue 1 , January 1980 , pp. 107 - 113
Copyright
Copyright © The Nutrition Society 1980

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