Journal of Nutrition OpenSOurce Diets- www.ResearchDiets.com

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Journal of Nutrition Vol. 101 No. 4 April 1971, pp. 465-475
Copyright
This Article
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Loh, H. H.
Right arrow Articles by Berg, C. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Loh, H. H.
Right arrow Articles by Berg, C. P.

Production of D-Kynurenine and Other Metabolites from D-Tryptophan by the Intact Rabbit and by Rabbit Tissue1

Horace H. Loh and Clarence P. Berg2

Department of Biochemistry, College of Medicine, University of Iowa, Iowa City, Iowa 52240

Use of sensitive chromatographic techniques now available for the separation of D-kynurenine has shown that, contrary to earlier negative claims, it can be produced when D-tryptophan is administered parenterally to the rabbit or when it is incubated with liver preparations. D-Kynurenine is slowly convertible to kynurenic acid, both in the intact animal and by kidney homogenates. Conversion by purified D-amino acid oxidase is also possible, probably because the {alpha}-keto analog formed through deamination undergoes ring closure spontaneously. The striking production of indolepyruvic acid from D-tryptophan in the intact rabbit favors the probability that some of the kynurenic acid excreted may have arisen via L-tryptophan formed by inversion. Feeding polished rice undoubtedly induces incipient coenzyme deficiencies, but contrary to earlier claims, it failed to increase the excretion of kynurenine. It lowered the output of kynurenic acid and enhanced moderately the production of 3-hydroxykynurenine. Tests confirmed the presence of "D-tryptophan pyrrolase" in the small intestine and its capacity to attack both D- and L-tryptophan. Liver homogenates produced less kynurenine from D- than from L-tryptophan. Enantiomorphic identities were established chromatographically and by reaction with D- and L-amino acid oxidases.


1 The data presented are taken chiefly from a dissertation submitted by Horace H. Loh in partial fulfillment of requirements for the degree of Doctor of Philosophy in Biochemistry in the Graduate College of the University of Iowa. The financial aid given by U. S. Public Health Grants AM 01770 and AM 09797 from the National Institute of Arthritis and Metabolic Diseases is gratefully acknowledged. A resume of part of this study was presented before the American Society of Biological Chemists in Chicago, April 16, 1964. Cf. Loh, H. H., and C. P. Berg 1964 Metabolism of D-tryptophan. Federation Proc. 23: 421 (abstr. 1916).

2 Reprint requests should be sent to Clarence P. Berg at the address indicated.

Manuscript received 4 September 1970.


This article has been cited by other articles:


Home page
ScienceHome page
J. R. Carlson, M. T. Yokoyama, and E. O. Dickinson
Induction of Pulmonary Edema and Emphysema in Cattle and Goats with 3-Methylindole
Science, April 21, 1972; 176(4032): 298 - 299.
[Abstract] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]