title: Purification and characterization of a galactose-specific agglutinin from the haemolymph of the larval stages of the insect Calliphora vomitoria.
abstract: A lectin was isolated from the haemolymph of the blowfly larva Calliphora vomitoria. It agglutinated a variety of mammalian erythrocytes with varying specificities and was strongly inhibited by D-galactose and fetuin. The activity was also sensitive to chelators of metal ions, heating above 50 degrees C and proteolytic digestion. SDS-PAGE identified a glycoprotein with an Mr of 32,000 under reducing and nonreducing conditions which resolved to a band at pH 5.4 using isoelectric focusing. Using FPLC gel filtration the activity was isolated in a fraction with an Mr of 130,000. It is suggested that the native form of the molecule is a noncovalently associated tetramer.
authors.affiliation: Department of Biology, University College London, U.K.
authors.forename: A N
authors.initials: AN
authors.lastname: McKenzie
authors.forename: T M
authors.initials: TM
authors.lastname: Preston
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D004175:Diptera / Q000737:chemistry* / Q000254:growth & development; D004492:Edetic Acid / Q000494:pharmacology; D005690:Galactose / Q000494:pharmacology; D006386:Hemagglutination Tests; D006458:Hemolymph / Q000737:chemistry*; D006358:Hot Temperature; D007525:Isoelectric Focusing; D007814:Larva; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D051381:Rats; D000509:alpha-Fetoproteins / Q000494:pharmacology
chemical_list: D037102:Lectins; D000509:alpha-Fetoproteins; D004492:Edetic Acid; D005690:Galactose