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.
D000818:Animals; D002454:Cell Differentiation; D002642:Chick Embryo; D037102:Lectins / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000196:embryology* / Q000378:metabolism; D013997:Time Factors
D037102:Lectins