Abstract
Strong haemagglutinin activity (titre 512) toward vertebrate erythrocytes is present in the haemolymph of both sexes of the adult cricket Teleogryllus commodus (Walker). Affinity chromatography on Sepharose-fetuin was used to concentrate the activity 213-fold. The haemagglutinin is a high molecular weight, water-insoluble protein which decreases in stability during purification. Purified activity is lost or diminished upon lyophilization, ultrafiltration, dialysis, heating, freezing, EDTA or trypsin treatment. In contrast, frozen crude haemolymph retains full activity for months. Insolubilized concanavalin A irreversibly absorbs the haemagglutinin activity independent of competing ligand. Human (ABO), chicken, pigeon and rat erythrocytes are strongly agglutinated, while sheep, cat and monkey red cells are weakly agglutinated. Horse and rabbit cells are not agglutinated by T. commodus haemagglutinin. Unpurified haemagglutinin activity is inhibited by low concentrations of fetuin and N-acetyl neuraminic acid. Purified activity is additionally inhibited by N- acetyl- d-glucosamine and N- acetyl- d-galactosamine . Bovine serum albumin, trehalose, sucrose, d-glucuronic acid and several other simple carbohydrates are non-inhibitory.
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