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Purification of the rabbit small intestinal sucrase-isomaltase complex: Separation from other maltases

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Abstract

The rabbit intestinal sucrase-isomaltase complex has been purified to homogeneity after solubilization with Triton X 100 followed by chromatography on DEAE Sepharose CL 6B and a second solubilization with papain. After hydrophobic chromatography on Octyl Sepharose CL 6B, separation from other contaminating maltases was achieved by gel filtration on Ultrogel ACA 22. The final enzyme was purified 390 fold, with a specific activity of about 10 units per mg protein.

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  1. Centre de Recherches sur la Nutrition, Centre National de la Recherche Scientifique, 9 rue J. Hetzel, 92190, Meudon, France

    Monique Vasseur

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  1. Monique Vasseur
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Vasseur, M. Purification of the rabbit small intestinal sucrase-isomaltase complex: Separation from other maltases. Biosci Rep 9, 341–346 (1989). https://doi.org/10.1007/BF01114686

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  • DOI: https://doi.org/10.1007/BF01114686

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