Purification and determination of the action pattern of Haliotis tuberculata laminarinase.

Lépagnol-Descamps, V; Richard, C; Lahaye, M; Potin, P; Yvin, J C; Kloareg, B

Lépagnol-Descamps, V; Richard, C; Lahaye, M; Potin, P; Yvin, J C; Kloareg, B.

Afiliación

Lépagnol-Descamps V; Centre d'Etudes d'Océanographie et de Biologie Marine (CEOBM-CNRS UPR 9042) B.P. 74, Roscof, France.

Carbohydr Res ; 310(4): 283-9, 1998 Aug.

Article en En | MEDLINE | ID: mdl-9821264

RESUMEN

The major laminarinase activity (EC 3.2.1.39) from the gastropodean marine mollusc Haliotis tuberculata was purified to homogeneity by cation exchange chromatography and its action pattern was investigated by HPAEC-PAD analysis of the degradation of various laminarin samples. It consists of a 60 kDa protein capable of depolymerizing the unbranched portions of the beta-(1-->3), beta-(1-->6)-glucan, down to laminaritriose. The enzyme operates via a molecular mechanism retaining the anomeric configuration. As the purified protein does not cleave the beta-(1-->6) linkages, it can be used for the structural analysis of laminarins.

Asunto(s)

Glucano Endo-1,3-beta-D-Glucosidasa/aislamiento & purificación; Moluscos/enzimología; Secuencia de Aminoácidos; Animales; Cromatografía por Intercambio Iónico; Hidrólisis; Datos de Secuencia Molecular; Polisacárido Liasas/aislamiento & purificación; Conformación Proteica

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glucano Endo-1,3-beta-D-Glucosidasa / Moluscos Límite: Animals Idioma: En Revista: Carbohydr Res Año: 1998 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Países Bajos

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