Porphyrin biosynthesis. Immobilized enzymes. IV. Studies on aminolaevulate dehydratase attached to Sepharose.
作者： Ana Maria Stella , Eva Wider de Xifra , Alcira M. del C. Batlle
DOI: 10.1007/BF01732049
关键词:
摘要: Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have studied. The optimal conditions for coupling determined. It was found that the immobilized enzyme retained a significant percentage of activity free enzyme. yield rather high. insolubilized requires both anaerobiosis thiol activator maximal activity. can be stored at 4 °C long periods with little loss it repeatedly used without alteration enzymic capacity. Attachment ALA-D gel led an enhanced thermal stability. pH optima bound same while small decrease in Km matrix bonded as compared soluble observed. use fixed-ALA-D preparation PBG is described.
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