Interaction of flavin mononucleotide with dimeric and tetrameric forms of muscle phosphorylase beta.
Biochimie
; 73(11): 1339-43, 1991 Nov.
Article
en En
| MEDLINE
| ID: mdl-1799627
Interaction of flavin mononucleotide (FMN) with dimeric and tetrameric forms of rabbit muscle glycogen phosphorylase beta has been studied under the conditions when allosteric activator binding sites are saturated by AMP (1 mM AMP; pH 6.8; 17 degrees C). Simultaneous use of schlieren optical system and photoelectric scanning absorption optical system of analytical ultracentrifuge Spinco, model E, makes it possible to register the oligomeric state of the enzyme and calculate the degree of saturation of individual oligomeric enzyme forms by FMN. The apparent association constant for the equilibrium dimer in equilibrium with tetramer decreased with increasing FMN concentration. The microscopic dissociation constants for the complexes of dimeric and tetrameric forms of glycogen phosphorylase beta with FMN have been found to be equal to 10 and 79 microM, respectively.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosforilasa b
/
Mononucleótido de Flavina
Límite:
Animals
Idioma:
En
Revista:
Biochimie
Año:
1991
Tipo del documento:
Article
Pais de publicación:
Francia