Affinity and hydrophobic interactions of penicillin amidase.
Hindustan Antibiot Bull
;
1989 Feb-May; 31(1-2): 25-8
Artículo
en Inglés
| IMSEAR
| ID: sea-2593
ABSTRACT
Binding of penicillin amidase from E. coli 436 to aniline-, benzylamine- and phenylethylamine-Sepharose was studied. Binding of the enzyme to aniline-Sepharose was exclusively due to hydrophobic interactions. Benzylamine-Sepharose binds the enzyme due to affinity interactions in the absence of ammonium sulphate and due to hydrophobic interactions in the presence of ammonium sulphate. A conformational change in the penicillin amidase molecule due to ammonium sulphate there by exposing the side chain binding site as a hydrophobic core is suggested.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Penicilina Amidasa
/
Fenetilaminas
/
Bencilaminas
/
Cromatografía de Afinidad
/
Amidohidrolasas
/
Compuestos de Anilina
Idioma:
Inglés
Revista:
Hindustan Antibiot Bull
Año:
1989
Tipo del documento:
Artículo
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