Regulatory features of glycogen phosphorylase from frog brain (Rana temporaria)
Tóm tắt
Từ khóa
Tài liệu tham khảo
Boron WF (1980) Intracellular pH regulation. In: Boulpaep EL (ed) Current Topics in Membranes and Transport. Academic Press, New York, pp 3–29
Brown GW (1964) The metabolism of Amphibia. In: Moore JA (ed) Physiology of the Amphibia. Academic Press, New York London, pp 1–98
Busby SJW, Radda GK (1976) Regulation of the glycogen phosphorylase system-from physical measurements to biological speculations. Curr Top Cell Res 10:89–160
Chapman AG, Westerberg E, Siesjö BK (1981) The metabolism of purine and pyrimidine nucleotides in rat cerebral cortex during insulin-induced hypoglycemia and recovery. J Neurochem 36:179–189
Chignell DA, Gratzer WB, Valentine RC (1968) Subunit interaction in native and modified muscle phosphorylase. Biochemistry 7:1082–1089
Cohen P, Duewer T, Fischer EH (1971) Phosphorylase from dogfish skeletal muscle. Purification and a comparison of its physical properties to those of rabbit muscle phosphorylase. Biochemistry 10:2683–2694
De Vincenzi DL, Hedrick JL (1970) Gel filtration, aggregation and the enzymatic activity of glycogen phosphorylase. Biochemistry 9:2048–2057
Dupre RK, Farrar ES (1982) Relationship of blood energy substrates and standard metabolic rate in several amphibian species. Comp Biochem Physiol 71A:627–629
Feldmann L, Zeisel J, Helmreich E (1972) Interactions between native and chemically modified subunits of matrix-bound glycogen phosphorylase. Proc Natl Acad Sci USA 69:2278–2282
Fischer EH, Krebs EG (1966) Relationship of structure to function of muscle phosphorylase. Fed Proc 25:1511–1520
Fischer EH, Heilmeyer LMG, Haschke RH (1971) Phosphorylase and the control of glycogen degradation. Curr Top Cell Reg 4:211–251
Fischer EH, Cohen P, Fosset M, Muir LW, Saari JC (1972) Comparative and evolutionary aspects of the control of phorphorylase. In: Wieland O, Helmreich E, Holzer H (eds) Second metabolic interconversion of enzymes. Springer, Berlin Heidelberg New York, pp 11–28
Fletterick RJ, Madsen NB (1980) The structures and related functions of phosphorylase a. Annu Rev Biochem 49:31–61
Foxon GEH (1964) Blood and respiration. In: Moore JA (ed) Physiology of the Amphibia. Academic Press, New York, London, pp 151–209
Gadian DG (1982) Nuclear magnetic resonance and its applications to living systems. Oxford University Press, Oxford New York
Hazel JR, Prosser CL (1974) Molecular mechanism of temperature compensation in poikilotherms. Physiol Rev 54:620–677
Hedrick JL, Shaltiel S, Fischer EH (1969) Conformational changes and the mechanism of resolution of glycogen phosphorylase b. Biochemistry 8:2422–2429
Hochachka PW, Somero GN (1984) Biochemical adaptation. Chapter 11: Temperature adaptation, pp 355–449. Princeton Univ. Press, Princeton, N.J.
Huhn H, Kamp G, Wegener G (1980) Der Einfluß von Umweltfaktoren auf den Glykogenstoffwechsel im Gehirn von Fröschen (Rana temporaria, R. esculenta). Verh Dtsch Zool Ges 1980:342
Jones DR (1967) Oxygen consumption and heart rate of several species of anuran Amphibia during submergence. Comp Biochem Physiol 20:691–707
Lowry OH, Passonneau JV, Hasselberger FX, Schulz DW (1964) Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain. J Biol Chem 239:18–30
Madsen NB, Cori CF (1956) The interaction of muscle phosphorylase with p-mercuribenzoate 1. Inhibition of activity and effect on the molecular weight. J Biol Chem 223:1055–1065
Metzger BE, Glaeser L, Helmreich E (1968) Purification and properties of frog skeletal muscle phosphorylase. Biochemistry 7:2021–2036
Rosenberg J (1935) Métabolisme du tissue nerveux de la grenouille “Rana esculenta L.” pendant le repos. Arch Intern Physiol 41:434–445
Satoh K, Imai F, Sato K (1978) A new glycogen phosphorylase present in the rat tissues containing the brain-type isozyme. The active monomer of brain-type isozyme. FEBS Lett 95:239–242
Shaltiel S, Hedrick JL, Fischer EH (1966) On the role of pyridoxal 5′-phosphate in phosphorylase; II. Resolution of rabbit muscle phosphorylase b. Biochemistry 5:2108–2116
Shaltiel S, Hedrick JL, Fischer EH (1969) Stereospecific reagents in the resolution and reconstitution of phosphorylase b. Biochemistry 8:2429–2436
Shaltiel S, Cortijo M, Zaidenzaig Y (1972) Probing and mapping the pyridoxal-5′-phosphate site of glycogen phosphorylase. In: Wieland O, Helmreich E, Holzer H (eds) Second Conference on Metabolic Interconversion of Enzymes. Springer, Berlin Heidelberg New York, pp 73–101
Somero GN, Hochachka P (1971) Biochemical adaptations to temperature in poikilotherms. Am Zool 11:159–167
Sudgen PH, Newsholme EA (1973) Activities of hexokinase, phosphofructokinase, 3-oxo acid coenzyme A-transferase and acetoacetyl-coenzyme A thiolase in nervous tissue from vertebrates and invertebrates. Biochem J 134:97–101
Thuy M, Wegener G (1983) Anoxieeffekte im Energiestoffwechsel des Grasfrosches. Hoppe-Seyler's Z Physiol Chem 364:1224–1225
Umminger BL (1977) Relation of whole blood sugar concentrations in vertebrates to standard metabolic rate. Comp Biochem Physiol 56A:457–460
Veech RL, Harris RL, Veloso D, Veech EH (1973) Freezeblowing: a new technique for the study of brain in vivo. J Neurochem 20:183–188
Veech RL, Lawson JWR, Cornell NW, Krebs HA (1979) Cytosolic phosphorylation potential. J Biol Chem 254:6538–6547
Wegener G (1981) Comparative aspects of energy metabolism in nonmammalian brains under normoxic and hypoxic conditions. In: Stefanovich V (ed) Animal models and hypoxia. Pergamon Press, Oxford, pp 87–109
Wegener G, Zebe E (1971) Zum Energiestoffwechsel des Gehirns. Eine vergleichende Untersuchung an Vertretern der verschiedenen Wirbeltieklassen. Z Vergl Physiol 73:195–208
Wieser W (1973) Temperature relations of ectotherms: A speculative review. In: Wieser W (ed) Effects of temperature on ectothermic organisms. Springer, Berlin Heidelberg New York, pp 1–23
Winterstein H (1929). Der Stoffwechsel des Zentralnervensystems. In: Bethe A, von Bergmann G, Emben G, Ellinger A (eds) Handbuch der normalen und pathologischen Physiologie, Bd 9. Springer, Berlin, pp 515–611