Purification, characterization and localization of an endogenous lectin from quail intestine
Soluble extracts of quail intestinal mucosa contain a lectin activity specific for chicken and rabbit, trypsinized?? glutaraldehyde-fixed erythrocytes. This lectin activity could be totally inhibited by lactose and mucin. Quail lectin was first purified by affinity chromatography on either asialofetuin-Sepharose or mucin-Sepharose, followed by DEAE-Sepharose chromatography. Silver stains of SOS-PAGE revealed a single 14.5 kDaprotein. Gel filtration on Sephadex G-200 also yielded an apparent molecular weight of 14.5 kDa. suggesting the lectin is in a monomeric form. Isoelectric focusing of purified quail gut lectin resulted in its separation into a major band at pl 6.2 and four trace bands at 6.25, 6.27, 6.38 and 6.45. Immunochemical localization of quail gut lectin in the intestine was carried out with polyclonal antibody raised in rabbits and tested for specificity on Western blots. Immunohistochemical staining showed that the lectin is present in the secretion coating the mucosal surface of the small bowel and in goblet cells. Lectin could be purified from all sections of intestine and localized to goblet cells in all cases.
Bibliography: p. 94-104.
Fang, R. (1989). Purification, characterization and localization of an endogenous lectin from quail intestine (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/23813