Purification of indolyl-3-alkane alpha-hydroxylase by affinity chromatography on indolyl-agarose columns.
Biochim Biophys Acta
; 527(1): 264-71, 1978 Nov 10.
Article
en En
| MEDLINE
| ID: mdl-718963
ABSTRACT
Indolyl-3-alkane alpha-hydroxylase was isolated from soil isolate organism, Pseudomonas XA, by affinity chromatography on indolyl-agarose, using different indole derivatives (L-tryptophan, N-acetyl-L-tryptophan, indole-3-carboxaldehyde and 3-indole-acrylic acid). With the exception of N-acetyl-L-tryptophan-agarose, excellent yields were obtained. The affinity chromatography step caused a 15-fold increase in the specific activity of the enzyme. The purity of indolyl-3-alkane alpha-hydroxylase was comparable to the preparations obtained by conventional isolation techniques; however, it showed a 7- to 10-times higher overall yield. Affinity purified indolyl-3-alkane alpha-hydroxylase exhibited essentially one band in polyacrylamide gel electrophoresis and on isoelectric focusing.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Oxigenasas de Función Mixta
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1978
Tipo del documento:
Article