Purification of indolyl-3-alkane α-hydroxylase by affinity chromatography on indolyl-agarose columns
| Autor: | Gottfried Schmer, Joseph Roberts |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Indole test
Indoles Chromatography Isoelectric focusing Sepharose Ion chromatography Tryptophan General Medicine Displacement chromatography Chromatography Affinity Mixed Function Oxygenases chemistry.chemical_compound Affinity chromatography chemistry Pseudomonas Agarose Polyacrylamide gel electrophoresis |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 527:264-271 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(78)90276-0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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