Abstract
Two lectins specific for D-galactosides with MW 31,000 and 34,000 (estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, under reduced conditions) were purified from coelomocytes of the echiuran, U. unicinctus. They were eluted together from a Bio-Gel P-100 column as a single peak with an apparent MW of 35,000. They closely resembled each other in saccharide specificity, isoelectric point and electrophoretic mobility under unreduced conditions. The hemagglutinating activity of both lectins was inhibited by a glycoconjugate fraction obtained from the Pronase-digest of coelomocytes.

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