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. 1969 Jun;113(1):49–55. doi: 10.1042/bj1130049

Purification and properties of α-galactosidases from Vicia faba seeds

P M Dey 1, J B Pridham 1
PMCID: PMC1184603  PMID: 5806396

Abstract

Two forms of α-galactosidase, I and II, exist in Vicia faba seeds and these have been purified 3660- and 337-fold respectively. They behaved as homogeneous preparations when examined by ultracentrifugation, disc electrophoresis and gel filtration. The apparent molecular weights of enzymes I and II, as determined by gel filtration, were 209000 and 38000 respectively. The carbohydrate contents of enzymes I and II were 25% and 2·8% respectively, and the enzymes differed in their aromatic amino acid compositions. Enzyme I was split into six inactive subunits in the presence of 6m-urea. α-Galactosidases I and II showed different pH optima and Km and Vmax. values with p-nitrophenyl α-d-galactoside and raffinose as substrates, and also differed in their thermal stabilities.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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