Comparison of lectin receptor and membrane coat-associated glycoproteins of milk lipid globule membranes.
1. Glycoproteins of bovine (Bos taurus) and human (Homo sapiens) milk lipid globule membranes were characterized by ability to bind lectins after electrophoretic separation. 2. Seven lectin receptor glycoproteins were detected in bovine and five in human milk lipid globule membranes. Bovine and human globule membrane glycoproteins differed in ability to interact with certain lectins. 3. Two major nonionic detergent insoluble glycoproteins were present in bovine and human lipid globule membrane; these constituents had apparent molecular weights of 155,000 and 69,000. Detergent-insoluble polypeptides with similar or identical electrophoretic mobilities were found in milk lipid globule membranes from four other species, rat (Rattus norvegicus), sheep (Ovis aries), pig (Sus scrofa) and goat (Capra hircus). Tryptic peptide mapping revealed these polypeptides to be nonidentical among species.
D000818:Animals; D000941:Antigens / Q000302:isolation & purification*; D002417:Cattle; D005260:Female; D006801:Humans; D008562:Membrane Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D008892:Milk / Q000276:immunology; D008895:Milk, Human / Q000276:immunology; D018396:Mucin-1; D051381:Rats; D011975:Receptors, Mitogen / Q000378:metabolism*
D000941:Antigens; D008562:Membrane Glycoproteins; D018396:Mucin-1; D011975:Receptors, Mitogen