Ceri, HowardFang, Rixun2005-07-212005-07-211989Fang, 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/238130315542179http://hdl.handle.net/1880/21543Bibliography: p. 94-104.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.xii, 104 leaves : ill. ; 30 cm.engUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.QP 552 L42 F36 1989Lectins - ResearchPurification, characterization and localization of an endogenous lectin from quail intestinemaster thesis10.11575/PRISM/23813QP 552 L42 F36 1989