Characterization of Korean native goat lactoferrin

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Title
Characterization of Korean native goat lactoferrin
Author(s)
Myoung Soo Nam; Kei-ichi Shimazaki; Haruto Kumura; Kyung Kwang Lee; Dae Yeul Yu
Bibliographic Citation
Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, vol. 123, pp. 201-208
Publication Year
1999
Abstract
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 sulfate-polyacrylamide gel electrophoresis and Western blot analysis suggested the molecular mass of Korean native goat lactoferrin is 82 kDa with an iron saturation of 30% as estimated by spectroscopic analysis. Circular dichroism analysis shows goat lactoferrin molecule contains 24.5%, α-helix; 36.0%, β-structure; 13.5%, β-turn and 26.0%, unordered structure. Heparin binding affinity is the same as that of bovine lactoferrin, but lower than that of human lactoferrin. An analysis using synthetic peptides shows that the peptide from residue 22 to 31-WQRRMRKLGA-exerts a positive heparin-binding ability.
Keyword
Korean native goatLactoferrinConformationHeparin-binding affinityIron-binding proteinCircular dichroismSecondary structureMilk protein
ISSN
0305-0491
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/S0305-0491(99)00060-7
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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