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. 1991 Dec 31;181(3):1564-71.
doi: 10.1016/0006-291x(91)92117-3.

Purification and characterization of a Coffea canephora alpha-D-galactosidase isozyme

F Haibach  1 , J Hata, M Mitra, M Dhar, M Harmata, P Sun, D Smith
Affiliations

Purification and characterization of a Coffea canephora alpha-D-galactosidase isozyme

F Haibach et al. Biochem Biophys Res Commun. .

Abstract

Exoglycosidases modify carbohydrate epitopes on glycoproteins and glycolipids. The alpha-D-galactosidase from Coffea canephora is an important exoglycosidase which degrades the human blood group B epitope. Although multiple isozymes have been described, they have never been demonstrably purified and thoroughly characterized. We have developed a technique to purify an isozyme to homogeneity. The isolated enzyme has a molecular weight of 36.7 kDa by SDS PAGE and 34.0 kDa by gel filtration. The isozyme is highly selective for alpha-D-galactosides and inactive against other low molecular weight substrates. It hydrolyzes the the terminal alpha-D-galactosyl residue from the blood group B epitope. Protease activity is below detectable limits. The isozyme has a broad pH optima at 6.3, a pl of 7.03, is unaffected by ionic strength, and is stable at 4 degrees C.

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