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- W1728705086 abstract "An α-galactosidase [EC 3.2.1.22] was isolated from the fruit of the watermelon, Citrullus battich. The enzyme was purified by procedures including extraction, ammonium sulfate precipitation, and chromatographies on DEAE-Sephadex, CM-Sephadex and Sephadex G-100. The final preparation was found to be fairly homogeneous on disc and SDS-polyacrylamide gel electrophoresis, and sufficiently free from other glycosidase activities. The molecular weight of the enzyme was estimated to be 45,000 by Sephadex G-100 column chromatography and SDS-polyacrylamide gel electrophoresis. The enzyme was most active at pH 4.5 for natural substrates and at 5.9 for artificial substrates. The enzyme liberates the α-galactose units from oligosaccharides of the raffinose series and ceramide trihex oside, and the hemagglutination-inhibiting activities of human ovarian cyst B-glycoprotein and blood group B-type ghosts were abolished by the enzyme." @default.
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- W1728705086 date "1986-01-01" @default.
- W1728705086 modified "2023-09-23" @default.
- W1728705086 title "Purification and Characterization of α-Galactosidase from Watermelon" @default.
- W1728705086 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a135465" @default.
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