Isolation and purification of amyloglucosidase from Halobacterium sodomense.
Biomed Chromatogr
; 7(5): 256-61, 1993.
Article
en En
| MEDLINE
| ID: mdl-8305855
Amyloglucosidase from Halobacterium sodomense was purified by a combination of hydrophobic interaction chromatography and immobilized metal ion affinity chromatography at analytical and preparative scale with 75% recovery. The enzyme was found to be a dimer of two different subunits with molecular weights of 72,000 and 82,000 D, respectively, combining in a 175,000 D native protein. The specific activity, KM, and amino acid composition of the enzyme was determined.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Glucano 1,4-alfa-Glucosidasa
/
Halobacterium
Idioma:
En
Revista:
Biomed Chromatogr
Año:
1993
Tipo del documento:
Article
País de afiliación:
Suecia
Pais de publicación:
Reino Unido