Characterization of Korean native goat lactoferrin.
Comp Biochem Physiol B Biochem Mol Biol
; 123(2): 201-8, 1999 Jun.
Article
en En
| MEDLINE
| ID: mdl-10425724
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%, alpha-helix; 36.0%, beta-structure; 13.5%, beta-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.
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Bases de datos:
MEDLINE
Asunto principal:
Lactoferrina
Límite:
Animals
País/Región como asunto:
Asia
Idioma:
En
Revista:
Comp Biochem Physiol B Biochem Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Japón