By Mary L. C. Bernheim(auth.)
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): ok. 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 relevant fearful method (pages 49–59): J. I. Salach, T. P. Singer, ok. 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 requisites for Amine Metabolism in vivo (pages 83–103): Theodore L. Sourkes and Krystyna Missala
Chapter 7 Physiological elements 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 medicinal drugs for comparing Pharmacological and Physiological Mechanisms (pages 163–179): Norton H. Neff and Jose A. Fuentes
Chapter 10 The half performed via Mono Amine Oxidase within the Inactivation of Catecholamines in Intact Tissues (pages 181–201): U. Trendelenburg, okay. H. Graefe and M. Henseling
Chapter eleven Can the Intra? and Extra?Homoneuronal Metabolism of Cate?Cholamines be unique within the Mammalian imperative apprehensive procedure? (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 advent to medical elements of Monoamine Oxidase Inhibitors within the therapy of melancholy (pages 271–296): C. M. B. Pare
Chapter 15 the connection among type and reaction to medications in Affective Disorders—Problems Posed via Drug reaction in Affective issues (pages 297–325): M. Roth, C. Gurney, C. Q. Mountjoy, T. A. Kerr and ok. Schapira
Chapter sixteen diversifications in Monoamine Oxidase job in a few Human ailment States (pages 327–340): M. Sandler
Chapter 17 medical, Genetic, Hormonal and Drug affects at the task of Human Platelet Monoamine Oxidase (pages 341–351): Dennis L. Murphy
Chapter 18 An research of Platelet Monoamine Oxidase task 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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Extra resources for Ciba Foundation Symposium 39 - Monoamine Oxidase and its Inhibition
Sandier: Dr Murphy mentioned pargyline in connection with the inhibition of both A and B forms being necessary for activity in depression. The drug may, in fact, be predominantly a B inhibitor (McCauley & Racker 1973). Even so, it seems to share the ability of other M A 0 inhibitors to bring about a lightening of affect (Bucci & Saunders 1961; Bucci et al. 1962; Stern 1963), although this action has been somewhat upstaged by its antihypertensive effect. Tipton: The efficiency of the tricyclic antidepressants as monoamine oxidase inhibitors in vivo will depend on how effectively they are taken up into the cells and concentrated.
Since most of the work on this enzyme has used soluble preparations of the enzyme, I don’t think one can come to any firm conclusions about its importance in the intact cell. The interpretation of in viro inhibition data is very difficult because of the possibility that the amines are located at different sites and the existence of permeability barriers to the inhibitor. Youdim: On the question of whether one can distinguish A and B forms in riw, and whether the substrate of one form inhibits the other enzyme, we have begun to study monoamine oxidase in intact organs, including the rat lung, which we believe is closer to the h viva situation.
Acad. Sci. A. 58, 1168-1173 KEARNEY, E. , SALACH, J. I . , WALKER, W. , SENG,R. , ZESZOTEK, E. & SINGER, T. P. (1971) The covalently-bound flavin of hepatic monoamine oxidase. I . Isolation and sequence of a flavin peptide and evidence for binding at the 8a position. Eur. J. Biochem. 24, 321-327 MAYCOCK, A. L. (1975) Structure of a flavoprotein-inactivatormodel compound. J. Am. Chem. Soc. , ABELES, R. , SALACH, J. 1. &SINGER, T. P. (1976) Structure of the flavininhibitor adduct from monoamine oxidase.