Ciba Foundation Symposium 39 - Monoamine Oxidase and its by Mary L. C. Bernheim(auth.)

By Mary L. C. Bernheim(auth.)

Content:
Chapter 1 creation (pages 1–4): S. S. Kety
Chapter 2 the character and destinations of the a number of kinds of Monoamine Oxidase (pages 5–31): okay. F. Tipton, M. D. Houslay and T. J. Mantle
Chapter three The motion of Acetylenic Inhibitors on Mitochondrial Monoamine Oxidase: constitution of the Flavin website within the Inhibited Enzyme (pages 33–47): A. L. Maycock, Robert H. Abeles, J. I. Salach and Thomas P. Singer
Chapter four Cysteinyl Flavin in Monoamine Oxidase from the crucial worried approach (pages 49–59): J. I. Salach, T. P. Singer, okay. T. Yasunobu, N. Minamiurat and M. B. H. Youdim
Chapter five Monoamine Oxidase Inhibitors and the Transformation of Monoamine Oxidases (pages 61–81): V. Z. Gorkin
Chapter 6 dietary necessities for Amine Metabolism in vivo (pages 83–103): Theodore L. Sourkes and Krystyna Missala
Chapter 7 Physiological facets of the Oxidative Deamination of Monoamines (pages 105–133): M. B. H. Youdim and Margarethe Holzbauert
Chapter eight research of the Pharmacological results of Selective Monoamine Oxidase Inhibitors (pages 135–161): J. Knoll
Chapter nine using Selective Monoamine Oxidase Inhibitor medications for comparing Pharmacological and Physiological Mechanisms (pages 163–179): Norton H. Neff and Jose A. Fuentes
Chapter 10 The half performed by way of Mono Amine Oxidase within the Inactivation of Catecholamines in Intact Tissues (pages 181–201): U. Trendelenburg, ok. H. Graefe and M. Henseling
Chapter eleven Can the Intra? and Extra?Homoneuronal Metabolism of Cate?Cholamines be unique within the Mammalian primary fearful method? (pages 203–229): D. F. Sharman
Chapter 12 Use of a Behavioural version to check the motion of Monoamine Oxidase Inhibition in vivo (pages 231–245): A. Richard eco-friendly and Moussa B. H. Youdim
Chapter thirteen family members among the measure of Monoamine Oxidase Inhibition and a few Psychopharmacological Responses to Monoamine Oxidase Inhibitors in Rats (pages 247–270): L. Mai?tre, A. Delini?Stula and P. C. Waldmeier
Chapter 14 creation to medical elements of Monoamine Oxidase Inhibitors within the remedy of melancholy (pages 271–296): C. M. B. Pare
Chapter 15 the connection among type and reaction to medications in Affective Disorders—Problems Posed by means of Drug reaction in Affective problems (pages 297–325): M. Roth, C. Gurney, C. Q. Mountjoy, T. A. Kerr and ok. Schapira
Chapter sixteen adaptations in Monoamine Oxidase task in a few Human sickness States (pages 327–340): M. Sandler
Chapter 17 medical, Genetic, Hormonal and Drug impacts at the job of Human Platelet Monoamine Oxidase (pages 341–351): Dennis L. Murphy
Chapter 18 An research of Platelet Monoamine Oxidase job in Schizophrenia and Schizoaffective Psychosis (pages 353–388): I. Brockington, T. J. Crow, Eve C. Johnstone and F. Owen
Chapter 19 end (pages 389–391): S. S. Kety

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Example text

It should be remembered that clorgyline and deprenyl are irreversible inhibitors of monoamine oxidase. Thus if the enzyme is incubated with a molar excess of such an inhibitor one will eventually attain complete inhibition. The selectivity of these inhibitors arises because the two species are inhibited at markedly different rates (Tipton 1971) and one selects an incubation time such that one species is virtually completely inhibited whereas the other is scarcely affected at the ‘plateau’ inhibitor concentration.

The problem with perfusion experiments of the type you describe is that one has no idea of the concentrations of the amines in the vicinity of monoamine oxidase. Our results (Houslay & Tipton 1975) indicate that when the two enzyme species meet substrates for both of them there will be a ‘damping’ effect due to cross-inhibition. g. Collins rt al. 1972) may be due, at least in part, to such an effect. Oreland: The presence of A and B forms of M A 0 has not been demonstrated in all organs. Thus Hall rt al.

The problem with perfusion experiments of the type you describe is that one has no idea of the concentrations of the amines in the vicinity of monoamine oxidase. Our results (Houslay & Tipton 1975) indicate that when the two enzyme species meet substrates for both of them there will be a ‘damping’ effect due to cross-inhibition. g. Collins rt al. 1972) may be due, at least in part, to such an effect. Oreland: The presence of A and B forms of M A 0 has not been demonstrated in all organs. Thus Hall rt al.

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