Lectin activity in embryonic chick muscle: developmental regulation and preliminary purification.

Soluble extracts of embryonic chick pectoral muscle contain lectin activity. This activity is assayed by agglutination of trypsin-treated, glutaraldehyde-fixed rabbit erythrocytes, and is blocked by specific saccharides such as thiodigalactoside and lactose. Lectin activity of the muscle extracts increased at least 1 order of magnitude between 8 and 16 days of chick embryo development, as the pectoral muscle differentiated. Preliminary purification was achieved by affinity chromatography on Sepharose 4B deprivatized with either asialo-bovine glycoprotein, or p-aminophenyl beta-D-thiogalactopyranoside as the ligand.