title: Enzymological investigations on the causes for the PSE-syndrome, II. Comparative studies on glycogen phosphorylase from pig muscles.
abstract: In order to investigate the cell biological causes for the fast breakdown of glycogen which is observed during the development of the PSE (pale, soft, exudative) syndrome in muscles of stress-susceptible pigs, muscle glycogen phosphorylase (GP) as a key enzyme in two isoforms, a and b, of the energy turnover was isolated from M. longissimus dorsi of normal and PSE-prone pigs of the German Landrace. GP b as well as GP a from normal and PSE-muscles exist in a dimeric form with a molecular weight of 97 000 D per subunit. The tendency for tetramerization of GP b increases in the presence of ATP, whereas the enzyme activity is simultaneously inhibited. The catalytic activities of GP a and GP b from both groups of animals show an optimum at pH 7.0. GP b can be activated to GP a by phosphorylation with the result of a 25% higher optimum specific activity in the case of normal and PSE-muscles. In interaction with glycogen and glucose-1-phosphate GP b follows the characteristics of a Michaelis-Menten kinetic, whereas the binding of AMP and phosphate proves to be allosteric. In comparison of the structural and kinetic characteristics of GP from normal as well as PSE-muscles no significant differences could be determined, indicating that GP does not belong to those factors which are triggering an accelerated energy turnover of ATP in muscles of stress-susceptible pigs.
authors: Institut für Chemie und Physik, Bundesanstalt für Fleischforschung, E.-C.-Baumann-Strasse 20, D-95326 Kulmbach, Germany.
authors: F
authors: F
authors: Schwägele
authors: P L
authors: PL
authors: Buesa
authors: K O
authors: KO
authors: Honikel