Wistaria sinensi agglutinin: Purification, carbohydrate specificity, and characterisation of the combining site
✍ Scribed by Hafiz Ahmed; Bishnu P. Chatterjee
- Book ID
- 102994710
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 763 KB
- Volume
- 177
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
A 2-acetamido-2-deoxy-D-galactose-binding agglutinin from Wistaria sinensis seeds, purified by affinity chromatography on a 2-acetamido-2-deoxy-D-galactose-starch conjugate, was homogeneous as judged by poly(acrylamide) disc gel electrophoresis. It had a mol. wt. of 66,000 (gel filtration on Sephadex G-150); on electrophoresis on SDS-poly(acrylamide) gel in the presence of 2-mercaptoethanol, it dissociated into sub-units of mol. wt. 34,000, suggesting the agglutinin to be a dimer; and it was a glycoprotein containing 4.8% of carbohydrate. It agglutinated several vertebrate erythrocytes, including human regardless of the blood group. In hapten-inhibition assays, 2-acetamido-2-deoxy-D-galactose and its glycosides were found to be better inhibitors than D-galactose and its glycosides, but N-acetyl-lactosamine was the most potent inhibitor. The binding involved HO-3,4 of the haptens and HO-2 partially.