HEMAGGLUTININS FROM OYSTER HEMOLYMPH

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Abstract
Oyster hemolymph hemagglutinin agglutinated fish, rabbit, and human, red blood cells, was active over a wide pH range (optimum pH 7.5), and was heat-labile. Dialysis caused a greater reduction in the activity in the aged hemolymph than it did in the fresh hemolymph. Ultracentrifugation removed 90% of the protein; the remaining 11% retained all the activity. Gel filtration revealed two distinct hemagglutinins associated with two main protein peaks. Fractionation according to solubility gave seven different protein fractions, but only the salt-soluble and a very minor water-soluble Fraction possessed hemagglutinating activity. Agar-gel diffusion tests on the protein fractions showed a complexity of patterns which was partially resolved by immunoelectrophoretic techniques.