N-acetyl-galactosamine-specific lectin, a novel lectin in the haemolymph of the ascidian Halocynthia roretzi: isolation, characterization and comparison with galactose-specific lectin
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説明
Abstract 1. 1. An N-acetyl-galactosamine-specific lectin has been isolated from haemolymph of the ascidian Halocynthia roretzi in an electrophoretically homogenous form, by four chromatographic operations including affinity chromatography on p- aminophenyl -N- acetyl-β- d -galactosaminide-Sepharose . 2. 2. The lectin has the mol. wt of 500,000 and the apparent sedimentation coefficient of 16–19 S. It is composed of subunits with a mol. wt of 28,000. 3. 3. The haemagglutinating activity of the lectin is Ca2+-dependent and inhibited with N- acetyl- d -galactosamine and its analogs. 4. 4. The lectin is adsorbed to a column of phenyl-Sepharose and eluted with 66% ethylene glycol. 5. 5. The concentration of the lectin in the haemolymph, as well as that of the galactose-specific lectin found previously in the same source, remains unchanged in response to injection of horse erythrocytes. 6. 6. Properties of the lectin is compared with those of the galactose-specific lectin.
収録刊行物
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- Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 88 (1), 375-381, 1987-01
Elsevier BV
