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Characterization and Proteolytic Origins of Specific Peptides Appearing During Lipopolysaccharide Experimental Mastitis

F. Moussaoui^*, F. Laurent^*, J. M. Girardet, G. Humbert, J-L. Gaillard and Y. Le Roux^*

^* Laboratoire de Sciences Animales, U.C. INRA 12 340, Ecole Nationale Supérieure d’Agronomie et des Industries Alimentaires (ENSAIA), 54 505 Vandoeuvre-lès-Nancy, France
Laboratoire des BioSciences de l’Aliment, U. C. INRA 885, Faculté des Sciences et Techniques, UHP - Nancy 1, 54 506 Vandoeuvre-lès-Nancy, France

Corresponding author:
F. Moussaoui; e-mail:
fatima.moussaoui{at}ensaia.nancy-inpl.fr.

Based on the compositional change of the proteose peptone fraction, proteolysis was studied over time following lipopolysaccharide-induced experimental mastitis. Electrophoresis of the proteose peptone fraction revealed many degradation products. Five peptides were identified by amino-terminal sequencing as internal fragments of ß-, -, _s1-, and _s2-casein that were generated by somatic cell proteases. Although -casein is considered particularly resistant to endogenous proteolysis, a -casein peptide was electrophoretically isolated in association with a ß-casein fragment. The in vitro kinetic studies of caseinate hydrolysis by elastase, one of the main polymorphonuclear neutrophil (PMN) proteases, suggested that the ß-casein peptide might be generated by elastase. In addition, elastase activity in milk PMN was higher during the inflammation of the mammary gland than prior to infusion.

Key Words: casein • endogenous proteolysis • lipopolysaccharide • mastitis

Abbreviation key: CAPS = 3-[cyclohexylamino]-1-propanesulfonic acid, GMP = glycomacropeptide, LPS = lipopolysaccharide, MM = molecular mass, PI = postinfusion, PMN = polymorphonuclear neutrophils, PP = proteose peptone

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