Preparation and properties of haemagglutinin from haemolymph of acrididae (Grasshoppers)
| Autor: | Mark R. Stebbins, Kenneth D. Hapner |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
chemistry.chemical_classification
animal structures Chromatography Hemagglutination biology viruses virus diseases Lectin Hemagglutinin Trypsin complex mixtures Biochemistry Amino acid chemistry.chemical_compound chemistry Affinity chromatography Glucosamine Insect Science Galactose medicine biology.protein Molecular Biology medicine.drug |
| Zdroj: | Insect Biochemistry. 15:451-462 |
| ISSN: | 0020-1790 |
| DOI: | 10.1016/0020-1790(85)90057-5 |
| Popis: | The proteinaceous haemagglutinin (lectin) present in the haemolymph of Melanoplus sanguinipes (F) has been isolated and biochemically characterized. The protein was purified to homogeneity by affinity chromatography on a column of Sepharose-galactose. The purified haemagglutinin accounted for all observed haemolymphatic haemagglutination activity. Gel filtration and electrophoresis showed the haemagglutinin to be a 600–700,000 mol. wt noncovalent aggregate of 70,000 mol. wt subunits. The 70,000 subunit contained two disulfide-linked polypeptide chains of mol. wt 40,000 and 28,000, respectively. The purified haemagglutinin contained all the common amino acids and had highest amounts of acidic residues and least amounts of methionine and glucosamine. Haemagglutination activity was stable at −20°C in the presence of d -galactose but was destroyed by treatment of the haemagglutinin with trypsin, heat or EDTA. Haemagglutination inhibition studies showed that low concentrations (≤5 mM) of either d -galactosidic or d -glucosidic carbohydrates were bound by the haemagglutinin and inhibited agglutination of human asialo-erythrocytes. The purified haemagglutinin was antigenic in rabbits. Comparative experiments showed that the haemagglutinin from M. differentialis (Thomas) was identical to that from M. sanguinipes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|