By Dr. W. Weyler (auth.), Prof. Dr. K. F. Tipton, Prof. Dr. M. B. H. Youdim, Dr. C. J. Barwell, Prof. Dr. B. A. Callingham, Dr. G. A. Lyles (eds.)

Monoamine oxidase performs a big function within the pathogenesis of neuropsychiatric issues together with depressive ailment, Parkinson´s illness and Alzheimer´s affliction. the hot new release of selective monoamine oxidase inhibitors, with out significant unwanted effects, has discovered a trendy position within the therapy of those ailments. a few of these medications could have neuroprotective job with customers for treating innovative neurodegenerative ailments. the amount provides a suite of study papers on monoamine oxidase and its inhibitors. the subject is handled from the viewpoint of chemistry, biochemistry, pharmacology, body structure, neurology and psychiatry. The e-book serves as a short and finished reference resource for acquiring the hottest information.

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Additional resources for Amine Oxidases: Function and Dysfunction: Proceedings of the 5th International Amine Oxidase Workshop, Galway, Ireland, August 22–25, 1992

Sample text

A. J Neural Transm (1994) [Suppl] 41: 35-39 © Springer-Verlag 1994 Some problems associated with measuring monoamine oxidase activity in the presence of sodium azide c. J. Barwell and S. A. Ebrahimi School of Pharmacy and Biomedical Sciences, University of Portsmouth, Portsmouth, United Kingdom Summary. The colourimetric assay of monoamine oxidase actIvIty, as hydrogen peroxide production, normally requires the use of sodium azide to inhibit breakdown of hydrogen peroxide by catalase. 5 mM. Catalase activity of isolated rat liver mitochondria could be eliminated with the irreversible inhibitor of catalase, 3-amino-1,2,4-triazole.

Discussion Colorimetric measurement of hydrogen peroxide with peroxidase and a reduced dye provides a simple and economical assay of MAO. , 1984). This sensitivity is similar to that of the widely used but more expensive radiometric assay (Tipton and Youdim, 1983). Catalase occurs in most mammalian tissues and when MAO is assayed in tissue homogenates and isolated mitochondrial fractions, this enzyme will normally be present. Consequently it must be inhibited to prevent loss of hydrogen peroxide and underestimation of MAO activity.

Each preparation de aminated both tyramine and benzylamine. Benzylamine deaminating activity, as a percentage of tyramine deaminating activity, was four times lower in guinea pig. It was inhibited in an essentially monophasic manner and (- )-deprenyl was the most potent inhibitor, as is shown in Fig. 2. A guinea pig preparation containing 50% MAO-B activity as defined by its sensitivity to c10rgyline with tyramine as substrate, deaminated tyramine and 5-HT at similar rates of; 52,300 ± 4,100 and 47,000 ± 3,000nmolh- l g liver-I, respectively.

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