Abstract
Enzyme activities involved in tryptophan metabolism along the kynurenine pathway were studied in male New Zealand white rabbits. Activities are expressed both as specific activity and per g of fresh tissue. Liver tryptophan 2,3-dioxygenase activity (TDO), when assayed in either the absence (holoenzyme) or presence of added haematin (apoenzyme), did not change. Therefore, in rabbit, TDO was present only in holoenzyme form. Small intestine indole 2,3-dioxygenase was significantly higher than liver TDO. Mitochondrial kynurenine 3-monooxygenase was higher in liver than in kidney. Kynureninase activity was similar in both tissues, whereas kynurenine-oxoglutarate transaminase was markedly higher in kidney than in liver. 3-Hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase activities were higher in kidney than in liver. However, the former enzyme showed much higher activity than the latter.
These findings suggest that, in rabbit, tryptophan is mainly metabolised along the kynurenine pathway although the apo-TDO enzyme is lacking, as high indole 2,3dioxygenase activity can obviate this lack.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
L. Musajo and C.A. Benassi, Aspects of disorders of the kynurenine pathway of tryptophan metabolism in manAdv. Clin. Chem. 763–135 (1964).
F.M. Chiancone, Enzymes of the tryptophan —> nicotinic acid pathway, in:Newer method of nutritional biochemistryedited by A.A. Albanese, Vol. 2 (Academic Press, New York, 1965), pp. 249–284.
J.M. Price, R.R Brown, N. Yess, Testing the functional capacity of the tryptophan-niacin pathway in man by analysis of urinary metabolitesAdv. Metab. Disorders 2159–225 (1965).
H. Wolf, Studies on tryptophan metabolism in man, Scand.J. Clin. Lab. Invest.Suppl. No.1361–186 (1974).
W.E. Knox and A.H. Mehler, The conversion of tryptophan to kynurenine in liver I. The coupled tryptophan peroxidase-oxidase system forming formylkynurenineJ. Biol. Chem. 187419–438 (1950).
K. Higuchi, S. Kuno, and O. Hayaishi, Enzymic formation of D-kynurenineFed. Proc. 22243 (1963).
O. Hayaishi, F. Hirata, M. Fujiwara, T. Ohnishi, and T. Nukiwa, Catalytic properties and reaction mechanism of indoleamine 2,3-dioxygenaseFEBS Proc. Meet. 40131–144 (1975).
A.H. Mehler and W.E. Knox, The conversion of tryptophan to kynurenine in the liver. Il. The enzymatic hydrolysis of formylkynurenineJ. Biol. Chem. 187431–438 (1950).
C.E. Dalgliesh and H. Tabechian, Comparison of the metabolism of uniformily14C-labelled L-phenylalanine, L-tyrosin and L-tryptophan in the rat,Biochem. J. 62625–633 (1956).
F.T. De Castro, J.M. Price, and R.R. Brown, Reduced triphosphopyridine-nucleotide requirement for the enzymatic formation of 3-hydroxykynurenine from L-kynurenineJ. Am. Chem. Soc. 782904–2905 (1956).
F.T. De Castro, R.R Brown, and J.M. Price, The intermediary metabolism of tryptophan by cat and rat tissue preparationsJ. Biol. Chem. 228777–784 (1957).
M. Mason, The kynurenine transaminase of rat kidneyJ. Biol. Chem. 211839–844 (1954).
Y. Kotake and Y.M. Nakayama, Über die Anthranilsäurebildung aus Kynurenin durch OrgansattHoppeSayler’s Z. Physiol. Chem. 27076–83 (1941).
Braunstein A.E., Goryochenkova E.V., Paskhinaja T.S., Enzymatic formation of alanine from L-kynurenine and L-tryptophan, the role of vitaminB6in this process,Biokhimya,14163–179 (1949).
O. Wiss, and H. Fuch, Über den Abbau von Kynurenin, Oxykynurenin und verwandten Substanzen durch RattenleberenzymExperientia(Basel)6472–473 (1950).
A.H. Mehler, Formation of picolinic and quinolinic acids following enzymatic oxidation of 3hydrozyanthranilic acidJ.Biol. Chem. 218241–254 (1956).
E. Ragazzi, C.L.V. Costa, L. Caparrotta, M. Biasiolo, A. Bertazzo, G. Allegri, Enzyme activities along the tryptophan-nicotinic acid pathway in alloxan diabetic rabbits.Biochim. Biophys. Acta 1571 9–17 (2002).
O.H. Lowry, N.J. Rosebrough, A.L. Farr, and R.J. Randall, Protein measurement with the Folin phenol reagentJ. Biol. Chem. 193265–275 (1951).
E.L. Hove, J.F. Herndon, VitaminB6deficiency in rabbits,J. Nair. 61127–136 (1957).
C.E. Hunt, D.D. Harrington, Nutrition and nutritional diseases of the rabbit, in:The biology of the laboratory rabbitedited by S.H. Weisbroth, R.E. Flatt, A.L. Krause (Academic Press, New York, 1974), pp. 403–433.
A. A-B. Badawy and M. Evans, Animal liver tryptophan pyrrolases. Absence of apoenzyme and of hormonal induction mechanism from species sensitive to tryptophan toxicityBiochem. J. 15879–88 (1976).
W.E. Knox and V.H. Auerback, The hormonal control of tryptophan peroxidase in the ratJ. Biol. Chem. 214 307–313 (1955).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2003 Springer Science+Business Media New York
About this chapter
Cite this chapter
Allegri, G., Ragazzi, E., Bertazzo, A., Biasiolo, M., Costa, C.V.L. (2003). Tryptophan Metabolism in Rabbits. In: Allegri, G., Costa, C.V.L., Ragazzi, E., Steinhart, H., Varesio, L. (eds) Developments in Tryptophan and Serotonin Metabolism. Advances in Experimental Medicine and Biology, vol 527. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0135-0_55
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0135-0_55
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4939-6
Online ISBN: 978-1-4615-0135-0
eBook Packages: Springer Book Archive