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

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 varieties 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 important apprehensive 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 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 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 uncommon within the Mammalian critical 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 relatives 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 points of Monoamine Oxidase Inhibitors within the therapy of melancholy (pages 271–296): C. M. B. Pare
Chapter 15 the connection among category and reaction to medicines 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 diversifications in Monoamine Oxidase task 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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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. Biochemistry 15, 114-125 MCEWEN,C. ,JR, SASAKI, G. & JONES,D. C. (1969) Human liver mitochondria1 monoamine oxidase.

C. (1969) Human liver mitochondria1 monoamine oxidase. 111. Kinetic studies concerning time-dependent inhibitors. Biochemistry 8, 3963-3972 PORTER, D. , VOET,J. G. & BRIGHT,H. J. (1973) Direct evidence for carbanions and covalent N5-flavin-carbanion adducts as catalytic intermediates in the oxidation of nitroethane by o-amino acid oxidase. J . Biol. Chem. 248, 4400-4416 RANW, R. R. (1973) 3-Bromoallylamine induced irreversible inhibition of monoamine oxidase. J . Am. C h m . Soc. 95, 4438-4439 RANDO,R.

1975) Inhibition of monoamine oxidase by propargylamine: structure of the inhibitor complex. Angew. Chem. Inr. Ed. Engl. , HEMMERICH, P. & MULLER,F. (1973) Studien in der FlavinReihe, XVIII. Die reduktive Alkylierung des Flavinkerns; Struktur und Reaktivitat von Dihydroflavinen. Liebigs Ann. Chern. 8, 1388-1415 L. & ERWIN,V. G. (1968) Mitochondria1 monoamine oxidase. 11. Action of HELLERMAN, various inhibitors for the bovine kidney enzyme. Catalytic mechanism. J . Biol. Chem. 243, 5234-5243 HEVESI,L.

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