Ovine lactoferrin: isolation from colostrum and characterization.
Highly purified lactoferrin was isolated from ovine colostrum by sequential purification on CM-Sephadex C-50 and Blue-Sepharose, with overall yield of 55%. The ovine lactoferrin was characterized by SDS-PAGE, its amino acid composition and N-terminal sequence to residue 30. Homology with bovine and human lactoferrins was greater than 80 and 50% respectively. Antibodies to ovine lactoferrin were raised in rabbits and used to develop an enzyme-linked immunosorbent assay (ELISA). The antiserum was not cross reactive with other colostrum proteins.
Buchta
R
R
Department of Immunology, John Curtin School of Medical Research, Australian National University, Canberra.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003126:Colostrum / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006801:Humans; D007106:Immune Sera / Q000276:immunology; D007781:Lactoferrin / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000737:chemistry; D012756:Sheep / Q000378:metabolism*
D000596:Amino Acids; D007106:Immune Sera; D007781:Lactoferrin