Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these select...
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| Autores principales: | , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella |
| Aporte de: |
| Sumario: | 1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these selective adsorbents is reported. These materials adsorb the enzyme quantitatively from partially purified preparations, and elution of delta aminolaevulinate dehydratase is achieved by modifying the ionic strength of the buffer. © 1977. |
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