Influence of detergents and pH on the isolation, purification and molecular properties of alpha-galactosidase-C2 from germinating guar (Cyamopsis tetragonolobus).
Indian J Biochem Biophys
;
1989 Aug; 26(4): 234-42
Artigo
em Inglês
| IMSEAR
| ID: sea-26845
ABSTRACT
alpha-Galactosidase was isolated from germinating guar. The extract also contained small amounts of alpha-mannosidase and beta-mannosidase activities. The fractionation of the enzyme extract with ammonium sulphate (75% saturation) resulted in the appearance of all the three enzymes in a floating lipid complex. The inclusion of detergents such as Triton X-100 and sodium deoxycholate in the extraction medium failed to prevent the appearance of these enzymes in the floating lipid complex. However, by using acetone powder of the seedlings, alpha-galactosidase could be sedimented with ammonium sulphate. The presence of detergents in the extraction medium affected the molecular properties of the enzyme. Using a set of carefully selected conditions alpha-galactosidase was purified to apparent homogeneity. Analytical ultracentrifugation and gel filtration studies of the purified enzyme showed association-dissociation phenomenon as a function of pH and temperature. The effect of pH on the association-dissociation indicates the predominance of electrostatic interactions in the association of subunits.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Plantas
/
Tensoativos
/
Química
/
Alfa-Galactosidase
/
Detergentes
/
Fenômenos Químicos
/
Galactosidases
/
Concentração de Íons de Hidrogênio
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1989
Tipo de documento:
Artigo
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