2006
DOI: 10.1016/j.idairyj.2005.01.009
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Variation in activity and heterogeneity of bovine milk proteases with stage of lactation and somatic cell count

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Cited by 38 publications
(33 citation statements)
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References 24 publications
(51 reference statements)
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“…During mastitis, the endogenous proteolytic activity in milk increases substantially [15,27,28] and it is known that plasmin can hydrolyse β-casein, α S2 -casein and α S1 -casein [29] which explains the presence of peptides from α S1 -casein and β-casein in milk from the infected group. The results presented here, from investigation of naturally occurring mastitis, are in agreement with investigations of experimental induction of mastitis with LTA [15] or lipopolysaccharide [28] in which plasmin activity in milk increased and casein derived peptides were identified by reverse phase HPLC [15] or 2 dimension electrophoresis and mass spectroscopy [28] during mastitis.…”
Section: Discussionmentioning
confidence: 99%
“…During mastitis, the endogenous proteolytic activity in milk increases substantially [15,27,28] and it is known that plasmin can hydrolyse β-casein, α S2 -casein and α S1 -casein [29] which explains the presence of peptides from α S1 -casein and β-casein in milk from the infected group. The results presented here, from investigation of naturally occurring mastitis, are in agreement with investigations of experimental induction of mastitis with LTA [15] or lipopolysaccharide [28] in which plasmin activity in milk increased and casein derived peptides were identified by reverse phase HPLC [15] or 2 dimension electrophoresis and mass spectroscopy [28] during mastitis.…”
Section: Discussionmentioning
confidence: 99%
“…It hydrolyses the four types of caseins and is capable of catalysing milk coagulation (Kaminogawa et al 1980;Larsen et al 1996;McSweeney et al 1995), which may explain the presence of clots in mastitic milk . Its level has been positively correlated with SCC (Larsen et al 2006;O'Driscoll et al 1999;Somers et al 2003). Procathepsin D, the proenzyme of cathepsin D, and cathepsin appear to have remained partially active after commercial pasteurization processes .…”
Section: Elastasementioning
confidence: 97%
“…Pyorala and Kaartinen (1988) found a decrease in plasmin activity during the transition from colostrum to milk. Larsen et al (2006) reported that the activity of the acid milk protease, cathepsin D, is significantly lower in colostrum than in milk.…”
Section: Proteinasesmentioning
confidence: 99%