Isolation and characterization of two individual glycoprotein components from human milk-fat-globule membranes.
Two individual glycoprotein components from human milk-fat-globule membranes (MFGM) has been purified by selectively extracting the membrane glycoproteins followed by lectin affinity chromatography and gel filtration on Sephadex G-200 in the presence of protein-disaggregating agents. The purified glycoprotein components, termed 'epithelial-membrane glycoprotein' (EMGP-155 and EMGP-39) have estimated molecular weights of 155 000 and 39 000 respectively, and yield a single band under reducing conditions on sodium dodecyl sulphate/polyacrylamide gel. EMGP-155 and EMGP-39 contain 21.0% and 7.0% carbohydrate by weight, with fucose (13.5%, 12.4%), mannose (3.7%, 6.2%), galactose (28.5%, 22.6%), N-acetylglucosamine (17.8%, 7.4%) and sialic acid (36.4%, 51.4%) of the carbohydrate moiety respectively. For both the glycoprotein components, aspartic and glutamic acid and serine are the major amino acid residues.
D000596:Amino Acids / Q000032:analysis; D000941:Antigens / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology / Q000302:isolation & purification*; D008895:Milk, Human / Q000032:analysis*; D018396:Mucin-1
D000596:Amino Acids; D000941:Antigens; D002241:Carbohydrates; D006023:Glycoproteins; D008565:Membrane Proteins; D018396:Mucin-1