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Title 

Characterization of Korean native goat lactoferrin

Authors 

Myoung Soo NamKei-ichi ShimazakiHaruto KumuraKyung Kwang LeeDae Yeul Yu

Publisher 

Elsevier

Issue Date 

1999

Citation 

Comparative Biochemistry & Physiology B, vol. 123, no. 0, pp. 201-208

Keywords 

Korean native goatLactoferrinConformationHeparin-binding affinityIron-binding proteinCircular dichroismSecondary structureMilk protein

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.

ISSN 

0305-0491

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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