Abstract
SummaryHighly 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.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Cited by
11 articles.
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