title: Purification and characterization of bovine lactoferrin from secretions of the involuting mammary gland: identification of multiple molecular weight forms.
abstract: 1. Lactoferrin was isolated from bovine mammary secretions collected during the nonlactating period. 2. A method utilizing heparin-agarose affinity chromatography was more efficient for purifying lactoferrin than a method including gel filtration, ion exchange chromatography and a second gel filtration. 3. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the purified lactoferrin was composed of two protein bands of apparent mol. wt. of 83,000 and 87,000. 4. Digestion with endoglycosidase H resolved the lactoferrin into two lower mol. wt. bands of 78,000 and 81,000. 5. The biochemical differences between the forms of lactoferrin are not exclusively due to differences in endoglycosidase H-sensitive oligosaccharide composition.
authors: Department of Animal Sciences, University of Illinois, Urbana 61801.
authors: J J
authors: JJ
authors: Rejman
authors: H M
authors: HM
authors: Hegarty
authors: W L
authors: WL
authors: Hurley
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005260:Female; D007781:Lactoferrin / Q000302:isolation & purification*; D007782:Lactoglobulins / Q000302:isolation & purification*; D008321:Mammary Glands, Animal / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight
chemical_list: D007782:Lactoglobulins; D007781:Lactoferrin