Characterization of Korean native goat lactoferrin

We purified lactoferrin from the colostrum of the Korean native goat (Capra hircus) by ion-exchange chromatography using CM-Toyopearl 650M followed by affinity chromatography on AF-Heparin Toyopearl 650M. Sodium dodecyl sulfa te-polyacrylamide gel electrophoresis and Western blot analysis suggested t he molecular mass of Korean native goat lactoferrin is 82 kDa with an iron saturation of 30%: as estimated by spectroscopic analysis. Circular dichroi sm analysis shows goat lactoferrin molecule contains 24.5%, alpha-helix; 36 .0%, beta-structure; 13.5%, beta-turn and 26.0%, unordered structure. Hepar in binding affinity is the same as that of bovine lactoferrin, but lower th an that of human lactoferrin. An analysis using synthetic peptides shows th at the peptide from residue 22 to 31 - WQRRMRKLGA - exerts a positive hepar in-binding ability. (C) 1999 Elsevier Science Inc. All rights reserved.