| A hemagglutinin (lectin) from the hemolymph of the blue crab, Callinectes sapidus, was isolated and characterized. The agglutinin molecule is made up of two different subunits; one has a molecular weight of 6.8 x 10('4) daltons, and the other 6.9 x 10('4) daltons. There are between 4 and 8 subunits per native agglutinin molecule (2-6 x 10('5) daltons MW).;The agglutinin does not exhibit Ca('++) or other divalent cation dependence for activity. Hemagglutination activity is inhibited by temperatures above 50 C. and by a pH below 5.5; optimal activity is between pH 6.0 and 7.0.;A crab serum free culture medium and system was developed which was capable of maintaining viable crab hemocytes for up to two weeks. A strontium chloride based anticoagulant, which prevented clotting of withdrawn hemolymph and was not cytotoxic to crab hemocytes, was also developed.;The agglutinin reacted with several saccharides: mannose, N-acetylglucosamine, N-acetylgalactosamine, fucose, N-acetylmannosamine and glucose. Saccharide specificity was determined by hemagglutination inhibition and mucin affinity column. Agglutination of the human erythrocytes tested does not depend on the ABO or Rh antigens. |
