Studies on influenza virus receptor-substance and receptor-substance analogues. 1. Preparation and properties of a homogeneous mucoid from the salivary gland of sheep

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Abstract
The isolation from the submandibular glands of sheep of a mucoprotein with high antihemagglutinin activity against influenza B virus is descr. The mucoprotein was homogeneous on electrophoretic and ultra-centrifugal examination. Analysis gave the following figures: N, 10.1; P, 0.4; S, 1.4 and fucose 1.1% . On acid hydrolysis 13.6% of reducing substances and 12.4% of hexosamine were released. The u.-v.-absorption spectrum indicated the presence of nucleic acid. One hexosamine was revealed by paper chromatography; the RF value was identical with that of galactosamine, but the nature of the hexosamine was not definitely established. The hydrolysate contained 10 amino acids. Agglutination of red cells by indicator influenza B (LEE) virus was inhibited by the purified mucoid at a concn. of 0.001 [mu]g./ml. Antihemagglutinin activity was lost on treating the mucoid with receptor-destroying enzymes, potassium periodate and trypsin. The relation of the mucoid to red-cell virus receptors and other soluble mucoid antihemag-glutinins is discussed. The molecular wt. of the mucoid calculated from sedimentation and diffusion data is 87,000 with a frictional ratio of 1.51. The mucoid is probably slightly polydis-perse and not greatly asymmetrical in molecular shape.