Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms

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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. In...

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Detalles Bibliográficos
Autores principales: Torres, H.N., Chelala, C.A.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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