| Literature DB >> 1662502 |
F Haibach1, J Hata, M Mitra, M Dhar, M Harmata, P Sun, D Smith.
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.Entities:
Mesh：
Substances：
Year: 1991 PMID： 1662502 DOI： 10.1016/0006-291x(91)92117-3
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575