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Comparison of immunomodulatory properties of purified lactoferrin, lactoperoxidase and β-casein in sheep

Published online by Cambridge University Press:  01 November 1998

CHUN W. WONG
Affiliation:
CSIRO Division of Animal Health, Armidale, NSW 2350, Australia
DENNIS L. WATSON
Affiliation:
CSIRO Division of Animal Health, Armidale, NSW 2350, Australia
GEOFFREY O. REGESTER
Affiliation:
Child Health Research Institute, North Adelaide, SA 5000, Australia
GEOFFREY W. SMITHERS
Affiliation:
CSIRO Division of Food Science and Technology, Highett, VIC 3190, Australia

Abstract

Bovine milk contains a variety of proteins and peptides that are biologically active (Ogra & Ogra, 1978; Duncan & McArthur, 1981; Newby et al. 1982; Juto, 1985; Stoeck et al. 1989; Mincheva-Nilsson et al. 1990; Watson, 1990; Barta et al. 1991; Politis et al. 1991; Fiat et al. 1993). Our laboratory has a long-term interest in some purified milk proteins, particularly lactoferrin (LF), lactoperoxidase (LP) and β-casein (β-CN), which have been shown to be immunologically significant. Some of our recent studies on these bovine milk proteins, particularly β-CN, indicated that their in vitro immunological effects did not always parallel their in vivo activities (Wong et al. 1996a, b; 1997a, b). This study was designed to investigate and compare the capacity of these purified bovine milk proteins to modulate a range of components that are vital to in vivo immune responses in sheep, with a view to providing further information on their potential in biomedical applications. To achieve this objective, a sensitive lymphatic cannulation model was employed that allows in vivo immune components and their functions to be measured in lymph collected under physiological conditions.

Type
SHORT COMMUNICATION
Copyright
Proprietors of Journal of Dairy Research 1998

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