Tripolyphosphatase associated with S-adenosylmethionine synthetase isozymes from rat liver.
Biochim Biophys Acta
; 883(2): 293-8, 1986 Sep 04.
Article
en En
| MEDLINE
| ID: mdl-3017437
ABSTRACT
S-Adenosylmethionine (AdoMet) synthetase alpha and beta were purified to homogeneity, as judged by SDS-polyacrylamide gel electrophoresis from rat liver. When the purified enzymes were applied onto Sephacryl S-200, each synthetase was eluted together with a tripolyphosphatase. The activities of these isozymes in synthesizing AdoMet and in hydrolyzing tripolyphosphate decreased in parallel with increasing amounts of rabbit anti-(beta-form) IgG. The activity of the beta-form isozyme was markedly stimulated by the addition of tripolyphosphate, whereas that of the alpha-form isozyme was inhibited. The tripolyphosphatase activity of both the alpha- and the beta-form was markedly stimulated by the addition of AdoMet. The tripolyphosphatases of each isozyme showed some other similar properties.
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Bases de datos:
MEDLINE
Asunto principal:
Transferasas
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Ácido Anhídrido Hidrolasas
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Monoéster Fosfórico Hidrolasas
/
Isoenzimas
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Hígado
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Metionina Adenosiltransferasa
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1986
Tipo del documento:
Article