Purification and properties of lung lectin. Rat lung and human lung beta-galactoside-binding proteins.
Lung is one of the organs of the rat with a particular abundance of haemagglutinating activity that is inhibited by beta-galactosides. This lectin activity can be attributed to a single protein that has been purified from rat lung; a similar protein has been purified from human lung. The molecular weights and subunit structures were estimated from gel filtration and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis; the human lung lectin appeared to be composed to two identical subunits, mol.wt. 14500, whereas rat lung lectin was observed as both a dimer and a tetramer of one subunit type, mol.wt. 13500. Both lectins bind to disaccharides or oligosaccharides with terminal beta-linked galactose residues. The carbohydrate moiety may be free [lactose or D-galactopyranosyl-beta-(1 leads to 4)-thiogalactopyranoside], protein-bound (asialofetuin) or lipid-bound (cerebrosides). The molecular properties of the beta-galactoside-binding proteins of rat lung and human lung are closely similar to those of embryonic chick muscle lectin [Nowak, Kobiler, Roel & Barondes (1977) Proc. Natl. Acad. Sci. U.S.A. 73, 1383--1387] and calf heart lectin [De Waard, Hickman & Kornfeld (1976) J. Biol. Chem. 251, 7581--7587].
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D005260:Female; D005697:Galactosides / Q000302:isolation & purification* / Q000378:metabolism; D037161:Galectins; D006027:Glycosides / Q000302:isolation & purification*; D006384:Hemagglutination / Q000187:drug effects; D006801:Humans; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D008168:Lung / Q000032:analysis* / Q000276:immunology; D009961:Orosomucoid / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D051381:Rats
D000596:Amino Acids; D002352:Carrier Proteins; D005697:Galactosides; D037161:Galectins; D006027:Glycosides; D037102:Lectins; D009961:Orosomucoid