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Ovine lactoferrin: isolation from colostrum and characterization

Published online by Cambridge University Press:  01 June 2009

Richard Buchta
Richard Buchta
Affiliation:
Department of Immunology, John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia
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Summary

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 immuno-sorbent assay (ELISA). The antiserum was not cross reactive with other colostrum proteins.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 2 , May 1991 , pp. 211 - 218
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

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