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Download Ciba Foundation Symposium - Control of Glycogen Metabolism by W. J. Whelan, Margaret P. Cameron(auth.) PDF

By W. J. Whelan, Margaret P. Cameron(auth.)

Chapter 1 beginning feedback (pages 1–6): F. G. Young
Chapter 2 constitution of Glycogen and Its Amylolytic Degradation (pages 7–28): Dexter French
Chapter three actual features of Undegraded Glycogen (pages 29–52): Stanley A. Orrell, Ernest Bueding and Magdalena Reissig
Chapter four Intestinal Hydrolysis and Absorption of Glycogen?Derived Oligosaccharides (pages 53–67): Arne Dahlqvist
Chapter five function of Uridine Diphosphate Glucose within the Synthesis of Glycogen (pages 68–86): Luis F. Leloir
Chapter 6 Branching Enzyme (pages 87–93): Joseph Larner
Chapter 7 The constitution of Phosphorylases (pages 94–106): Edmond H. Fischer, Michael M. Appleman and Edwin G. Krebs
Chapter eight The effect of Phosphorylase at the constitution of Glycogen (pages 107–122): Barbara Illingworth, David H. Brown and Carl F. Cori
Chapter nine The Enzymic Debranching of Glycogen and the function of Transferase (pages 123–138): M. Abdullah, Pamela M. Taylor and W. J. Whelan
Chapter 10 The function of Oligo?1,4>1,4?Glucan? Transferase and Amylo?1,6?Gluco?Sidase within the Debranching of Glycogen (pages 139–150): David H. Brown and Barbara Illingworth
Chapter eleven The Mechanism of motion of Amylo?I.6?Glucosidase (pages 151–175): H. G. Hers, W. Verhue and Monique Mathieu
Chapter 12 Animal Tissue ??Amylase and Its function within the metabolism of Glycogen (pages 176–192): E. L. Rosenfeld
Chapter thirteen normal dialogue on easy strategies of Glycogen Metabolism (pages 193–199):
Chapter 14 Interconversion Reactions of Muscle Phosphorylases B and A (pages 200–210): Edwin G. Krebs, Carmen Gonzalez, Jerome B. Posner, David S. Love, Gloria E. Bratvold and Edmond H. Fischer
Chapter 15 law of Glycolysis in Skeletal Muscle (pages 211–232): Ernst Helmreich, Simon Karpatkin and Carl F. Cori
Chapter sixteen The mobile place of Adenyl Cyclase and Adenosine?3,5??Phosphate in Escherichia coli (pages 233–246): Earl W. Sutherland, Peter Davoren and Richard Makman
Chapter 17 Biochemical results of Adrenaline on Intestinal soft Muscle (pages 247–253): Ernest Bueding
Chapter 18 rules of Glycogenolysis in Muscle: influence of Glucagon and Anoxia on Glycogenolysis within the Perfused Rat middle; influence of Adenine Nucleotides, Glucose 6?Phosphate and Inorganic Phosphate on Muscle Phosphorylase task. (pages 254–272): H. E. Morgan and A. Parmeggiani
Chapter 19 Insulin and the regulate of UDPG???Glucan Transglucosylase task (pages 273–293): J. Larner, M. Rosell?Perez, D. L. Friedman and J. W. Craig
Chapter 20 attainable oblique results of Adrenaline on Glycogen Metabolism (pages 294–300): P. J. Randle
Chapter 21 Hexokinase and Glucokinase (pages 301–304): A. Sols
Chapter 22 scientific Manifestations of Glycogen garage ailments (pages 305–320): Rudi Schmid
Chapter 23 Glycogen garage ailment, style I (pages 321–335): D. J. Manners
Chapter 24 Glycogen garage ailments, varieties III, IV, and VI (pages 336–353): Barbara Illingworth and David H. Brown
Chapter 25 Glycogen garage sickness, sort II (pages 354–365): H. G. Hers
Chapter 26 Glycogen garage disorder, variety V (pages 366–376): Joseph Larner
Chapter 27 Glycogen Synthetase Deficiency (pages 377–386): J. Spencer?Peet, G. M. Lewis and ok. M. Stewart
Chapter 28 reports of garage illness Glycogens (pages 387–415): Ernest Bueding, Stanley A. Orrell and James Sidbury

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7). Under these conditions, the average molecular weight of the fraction on the right is progressively reduced. On incubation of the worms in a glucose-containing medium in uitro, the molecular weight of this fraction progressively increases. Such variations as a result of changes in the nutitional state of the organism 42 S. A . O R R E L L , J R . , E. B U E D I N G A N D M. R E I S S I G can hardly be considered the result of an artifact of the extraction procedure. The variations in the molecular weight spectrum of cold water-extractedglycogen as a function of the glycogen levels of the tapeworm H.

Biol. ,236,2854. COLUCCI, A. , ORBELL, S. , SAZ, H. , and BUEDING, E. (1963). Unpublished observations. DROCHMANS, P. (1963). In Biochemical Society Symposia No. 23 : Methods of separation of subcellular structures, p. 127. Cambridge Univ. Press. GREENWOOD, C. J. Roc. chem. , 26. LAZAROW, A. h u t . , 31. LELOIB,L. , and GOLDEMBERG, S. H. (I+). J. bid. , 235,919. LELOIR, L. , O L A V AJ. , A , GOLDEMBERG, S. H.. and CAFWNATTI, H. (1959). Arch. , 81, 508. ORRELL, S. , and BUEDING, E. J. h e r . chem.

Hehre and Hamilton (1951) have shown that an enzymic system fiom Acetobacter cupmlatum is capable of converting starch dextrins into a dextran containing mainly a-1 ,&linkages. On the other hand, Q-enzyme is capable of converting only a small fraction of a-1,4-linkages in amylose into a-I,Glinks. Since the limitation to further branching cannot be a thermodynamic one, it must stem &om the steric specificity of the enzyme. Similarly, a yeast branching enzyme, capable of converting amylopectin into a glycogen-like polysaccharide, has no appreciable action on glycogen itself (Gunja and Manners, 1959).

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