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Abstract:

1. 1. The inactivation of phosphorylase a phosphatase decreased the maximum velocity of the phosphorylase a to phosphorylase b conversion reaction when it was assayed at different phosphorylase a concectrations. 2. 2. Maximal phosphorylase a phosphatase activities were found between pH 8 and 8.3. Inactivation of the phosphorylase a phosphatase led to a decrease in the activity in all the pH ranges tested. 3. 3. Theophylline and caffeine stimulated the phosphorylase a phosphatase. The effect of these substances was exerted in the reaction assay of the enzyme. 4. 4. ATP, ADP, AMP, GTP, UTP, CTP and pyrophosphate were found to decrease the rate of the reaction catalyzed by phosphorylase a phosphatase. This effect showed a striking parallelism with the capacity of these compounds to stimulate the phosphatase inactivation. © 1970.

Registro:

Documento: Artículo
Título:Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
Autor:Torres, H.N.; Chelala, C.A.
Filiación:Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina
Palabras clave:adenine nucleotide; caffeine; glucosyltransferase; guanine nucleotide; phosphatase; phosphorus; pyrimidine nucleotide; pyrophosphate; theophylline; animal; article; chemistry; enzyme activation; enzymology; kinetics; muscle; pH; rabbit; Adenine Nucleotides; Animal; Caffeine; Chemistry; Cytosine Nucleotides; Diphosphates; Enzyme Activation; Glucosyltransferases; Guanine Nucleotides; Hydrogen-Ion Concentration; Kinetics; Muscles; Phosphoric Monoester Hydrolases; Phosphorus Isotopes; Rabbits; Theophylline; Uracil Nucleotides
Año:1970
Volumen:198
Número:3
Página de inicio:495
Página de fin:503
DOI: http://dx.doi.org/10.1016/0005-2744(70)90127-0
Título revista:BBA - Enzymology
ISSN:00052744
CAS:caffeine, 30388-07-9, 58-08-2; glucosyltransferase, 9031-48-5; phosphatase, 9013-05-2; phosphorus, 7723-14-0; pyrophosphate, 14000-31-8, 7722-88-5, 7758-16-9; theophylline, 58-55-9, 5967-84-0, 8055-07-0, 8061-56-1, 99007-19-9; Adenine Nucleotides; Caffeine, 58-08-2; Cytosine Nucleotides; Diphosphates; Glucosyltransferases, EC 2.4.1.-; Guanine Nucleotides; Phosphoric Monoester Hydrolases, EC 3.1.3; Phosphorus Isotopes; Theophylline, 58-55-9; Uracil Nucleotides
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00052744_v198_n3_p495_Torres.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n3_p495_Torres

Referencias:

  • Cori, Green, (1943) J. Biol. Chem., 151, p. 31
  • Graves, Fischer, Krebs, (1960) J. Biol. Chem., 235, p. 805
  • Fischer, Graves, Snyder Crittenden, Krebs, (1959) J. Biol. Chem., 234, p. 1698
  • Morgan, Parmeggiani, (1964) J. Biol. Chem., 239, p. 2435
  • Morgan, Parmeggiani, (1964) J. Biol. Chem., 239, p. 2440
  • Belocopitow, (1961) Arch. Biochem. Biophys., 93, p. 457
  • Craig, Larner, (1964) Nature, 202, p. 971
  • Posner, Stern, Krebs, (1965) J. Biol. Chem., 240, p. 982
  • Hammermeister, Yunis, Krebs, (1965) J. Biol. Chem., 240, p. 936
  • Torres, Maréchal, Bernard, Belocopitow, (1968) Biochim. Biophys. Acta, 156, p. 206
  • Riley, Haynes, (1963) J. Biol. Chem., 238
  • Merlevede, Riley, (1966) J. Biol. Chem., 241, p. 3517
  • Chelala, Torres, (1969) Biochim. Biophys. Acta, 178, p. 423
  • Lowenstein, Lardy, (1960) Biochemical Preparations, 7, p. 5. , Wiley, New York
  • Paladini, Leloir, (1952) Biochem. J., 51, p. 426
  • Chelala, Torres, (1968) Biochem. Biophys. Res. Commun., 32, p. 704
  • Fischer, Krebs, Colowick, Kaplan, (1962) Methods in Enzymology, 5, p. 369. , Academic Press, New York
  • Bray, (1960) Anal. Biochem., 1, p. 279
  • Cori, Illingworth, Keller, Colowick, Kaplan, (1955) Methods in Enzymology, 1, p. 200. , Academic Press, New York
  • Seery, Fischer, Teller, (1967) Biochemistry, 6, p. 3315
  • Chelala, Torres, (1970) Biochim. Biophys. Acta, 198, p. 504
  • Wosilait, Sutherland, (1956) J. Biol. Chem., 218, p. 469
  • Holmes, Mansour, (1968) Biochim. Biophys. Acta, 156, p. 266
  • Hurd, Novoa, Hickenbottom, Fischer, Neufeld, Ginsburg, (1966) Methods in Enzymology, 8, p. 546. , Academic Press, New York

Citas:

---------- APA ----------
Torres, H.N. & Chelala, C.A. (1970) . Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms. BBA - Enzymology, 198(3), 495-503.
http://dx.doi.org/10.1016/0005-2744(70)90127-0
---------- CHICAGO ----------
Torres, H.N., Chelala, C.A. "Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms" . BBA - Enzymology 198, no. 3 (1970) : 495-503.
http://dx.doi.org/10.1016/0005-2744(70)90127-0
---------- MLA ----------
Torres, H.N., Chelala, C.A. "Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms" . BBA - Enzymology, vol. 198, no. 3, 1970, pp. 495-503.
http://dx.doi.org/10.1016/0005-2744(70)90127-0
---------- VANCOUVER ----------
Torres, H.N., Chelala, C.A. Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms. 1970;198(3):495-503.
http://dx.doi.org/10.1016/0005-2744(70)90127-0