Heparin-inhibitable lectin. Purification from chicken liver and embryonic chicken muscle

The heparin-inhibitable lectin activity from adult chicken liver and embryonic chick pectoral muscle has been purified by gel filtration on Sepharose CL-2B followed by affinity chromatography on heparin-Sepharose. Specific activity of this abundant material was increased about 70-fold with about 28% recovery of activity. The purified lectin, which behaved as a large aggregate, could be dissociated into two proteins with apparent molecular weights of 13,000 and 16,000 upon electrophoresis in sodium dodecyl sulfate. 125I-tryptic peptide maps of these proteins showed that they were distinct from each other and also from lectins of similar molecular weight previously purified from chicken. Agglutination activity of the lectin, tested with specially prepared rabbit erythrocytes, was very sensitive to heparin which inhibited 50% at concentrations of approximately 10(-5) mM. Dermatan sulfate and heparan sulfate were also potent inhibitors, whereas other glycosaminoglycans were not. The most potent monosaccharide hapten inhibitor was N-acetyl-D-galactosamine. Because of its properties, we operationally refer to this material as chicken heparin-lectin, recognizing that this does not necessarily indicate that it functionally interacts with heparin in vivo.