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Inhibition of Tyrosine Aminotransferase by β‐ N ‐Oxalyl‐l‐α,β‐Diaminopropionic Acid, the Lathyrus sativus Neurotoxin by K. Shasi Vardhan; M. P. Pratap Rudra; S. L. N. Rao is a Neuroscience article available to read on EtoBox.

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Abstract: Species differences in susceptibility are a unique feature associated with the neurotoxicity of β‐__N__‐oxalyl‐l‐α,β‐diaminopropionic acid (l‐ODAP), the __Lathyrus sativus__ neurotoxin, and the excitotoxic mechanism proposed for its mechanism of toxicity does not account for this feature. The present study examines whether neurotoxicity of l‐ODAP is the result of an interference in the metabolism of any amino acid and if it could form the basis to explain the species differences in susceptibility. Thus, Wistar rats and BALB/c (white) mice, which are normally resistant to l‐ODAP, became susceptible to it following pretreatment with tyrosine (or phenylalanine), exhibiting typical neurotoxic symptoms. C57BL/6J (black) mice were, however, normally susceptible to l‐ODAP without any pretreatment with tyrosine. Among the various enzymes associated with tyrosine metabolism examined, the activity of only tyrosine aminotransferase (TAT) was inhibited specifically by l‐ODAP. The inhibition was noncompetitive with respect to tyrosine (__K__~i~ = 2.0 ± 0.1 m__M__) and uncompetitive with respect to α‐ketoglutarate (__K__~i~ = 8.4 ± 1.5 m__M__). The inhibition of TAT was also reflected

Who reads Inhibition of Tyrosine Aminotransferase by β‐ N ‐Oxalyl‐l‐α,β‐Diaminopropionic Acid, the Lathyrus sativus Neurotoxin?

Author

K. Shasi Vardhan; M. P. Pratap Rudra; S. L. N. Rao

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1997

Language

EN

Field

Neuroscience (Life Sciences)