Relationships between dephosphorylation and D to I conversion of rabbit skeletal muscle glycogen synthase.
J Biol Chem
; 253(15): 5247-50, 1978 Aug 10.
Article
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| ID: mdl-209031
ABSTRACT
The relationship between dephosphorylation and D to I conversion of skeletal muscle glycogen synthase by synthase phosphatase was investigated using synthase preparations containing 1 to 3 mol of 32P/mol of subunit (90,000 g). Dephosphorylation was analyzed in terms of 32P release from the trypsin-sensitive and trypsin-insensitive phosphorylation regions of synthase. With synthase containing 1 to 2 mol of 32P/90,000 g, dephosphorylation of the trypsin-insensitive region correlated closely with D to I conversion and was more rapid than dephosphorylation of the trypsin-sensitive region. Synthase containing 3 mol of 32P/90,000 g was a relatively poor substrate for the phosphatase since dephosphorylation of both regions, as well as D to I conversion, was slow. With this species of synthase, glucose-6-P (0.1 mM) increased the rates of D to I conversion and dephosphorylation of trypsin-insensitive region. It is concluded that dephosphorylation of the trypsin-insensitive region is responsible for the conversion of synthase D to I.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Glucógeno Sintasa
/
Glucógeno Sintasa-D Fosfatasa
/
Monoéster Fosfórico Hidrolasas
/
Músculos
Límite:
Animals
Idioma:
En
Revista:
J Biol Chem
Año:
1978
Tipo del documento:
Article