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Inhibition of the proteinase activity in mastitic milk

Published online by Cambridge University Press:  01 June 2009

Weihuan Fang  and
Markus Sandholm
Weihuan Fang
Affiliation:
Department of Pharmacology and Toxicology, Department of Veterinary Medicine, Hämeentie 57, FIN-00580 Helsinki, Finland
Markus Sandholm
Affiliation:
Department of Pharmacology and Toxicology, Department of Veterinary Medicine, Hämeentie 57, FIN-00580 Helsinki, Finland
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Summary

The antiproteolytic activity of selected proteinase inhibitors was studied in mastitic bovine milk and urokinase-activated normal milk using a caseolytic agar diffusion assay. The inhibition profiles of mastitic milk and urokinase-activated milk were compared with those of purified proteinases. The proteinase inhibition profile of mastitic milk did not resemble that of any of the pure proteinases, indicating a mixed type of proteinase system in mastitic milk. The trypanocidals diminazene (equivalent to Berenil®) and pentamidine (equivalent to Lomidine®), together with aprotinin (Trasylol®), showed most promise when considering possible applications in mastitis to break up the proteolytic cascade within the inflamed udder.

Type
Original articles
Information
Journal of Dairy Research , Volume 62 , Issue 1 , February 1995 , pp. 61 - 68
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

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References

REFERENCES

Andrews, A. T. 1983 a Proteinases in normal bovine milk and their action on caseins. Journal of Dairy Research 50–45Google ScholarPubMed
Andrews, A. T. 1983 b Breakdown of caseins by proteinases in bovine milks with high somatic cell counts arising from mastitis or infusion with bacterial endotoxin. Journal of Dairy Research 50 57–66CrossRefGoogle ScholarPubMed
De Koning, P. J., Kaper, J., Rollema, H. S. & Driessen, F. M. 1985 Age-thinning and gelation in unconcentrated and concentrated UHT-sterilized skim milk. Effect of native milk proteinase. Netherlands Milk and Dairy Journal 39 71–87Google Scholar
De Rham, O. & Andrews, A. T. 1982 a The roles of native milk proteinase and its zymogen during proteolysis in normal bovine milk. Journal of Dairy Research 49 577–585CrossRefGoogle ScholarPubMed
De Rham, O. & Andrews, A. T. 1982 b Qualitative and quantitative determination of proteolysis in mastitic milks. Journal of Dairy Research 49 587–596CrossRefGoogle ScholarPubMed
Kaartinen, L., Salonen, E. M., Vaheri, A. & Sandholm, M. 1988 a Activation of plasmin in mastitic milk. Acta Veterinaria Scandinavica 29 485–491CrossRefGoogle ScholarPubMed
Kaartinen, L. & Sandholm, M. 1987 Regulation of plasmin activation in mastitic milk. Correlation with inflammatory markers and growth of Streptococcus agalactiae. Journal of Veterinary Medicine B 34 42–50CrossRefGoogle ScholarPubMed
Kaartinen, L., Veijalainen, K., Kuosa, P. L., PyöRäLä, S. & Sandholm, M. 1988 b Endotoxin-induced mastitis. Inhibition of casein synthesis and activation of the caseinolytic system. Journal of Veterinary Medicine B 35 353–360CrossRefGoogle ScholarPubMed
Laskowski, M. & Laskowski, M. 1951 Crystalline trypsin inhibitor from colostrum. Journal of Biological Chemistry 190 563–573CrossRefGoogle ScholarPubMed
Lonsdale-Eccles, J. D. & Mpimbaza, G. W. N. 1986 Thiol-dependent proteases of African trypanosomes: analysis by electrophoresis in sodium dodecyl sulphate/polyacrylamide gels co-polymerized with fibrinogen. European Journal of Biochemistry 155 469–473CrossRefGoogle ScholarPubMed
Malkamäki, M., Mattila, T. & Sandholm, M. 1986 Bacterial growth in mastitic milk and whey. Journal of Veterinary Medicine B 33 174–179CrossRefGoogle ScholarPubMed
Mattila, T. & Frost, A. J. 1989 Induction by endotoxin of the inflammatory response in the lactating and dry bovine mammary gland. Research in Veterinary Science 46 238–240CrossRefGoogle ScholarPubMed
Mattila, T. & Sandholm, M. 1986 Milk plasmin,N-acetyl-β-D-glucosaminidase, and antitrypsin as determinants of bacterial replication rates in whey. Journal of Dairy Science 69 670–675CrossRefGoogle ScholarPubMed
Rawlings, N. D. & Barrett, A. J. 1990 Evolution of proteins of the cystatin superfamily. Journal of Molecular Evolution 30 60–71CrossRefGoogle ScholarPubMed
Richabdson, B. C. 1983 The proteinases of bovine milk and the effect of pasteurization on their activity. New Zealand Journal of Dairy Science and Technology 18 233–245Google Scholar
Saksela, O. 1981 Radial caseinolysis in agarose: a simple method for detection of plasminogen activator in the presence of inhibitory substances and serum. Analytical Biochemistry 111 276–282CrossRefGoogle ScholarPubMed
Sandholm, M. & Honkanen-Buzalski, T. 1979 Colostral trypsin-inhibitor capacity in different animal species. Acta Veterinaria Scandinavica 20 469–476CrossRefGoogle ScholarPubMed
Sandholm, M., Smith, R. R., Shih, J. C. H. & Scott, M. L. 1976 Determination of antitrypsin activity on agar plates: relationship between antitrypsin and biological value of soybean for trout. Journal of Nutrition 106 761–766CrossRefGoogle ScholarPubMed
Schaar, J. & Funke, H. 1986 Effect of subclinical mastitis on milk plasminogen and plasmin compared with that on sodium, antitrypsin and N-acetyl-β-D-glucosaminidase. Journal of Dairy Research 53 515–528CrossRefGoogle ScholarPubMed
Verdi, R. J. & Barbano, D. M. 1988 Preliminary investigation of the properties of somatic cell proteases. Journal of Dairy Science 71 534–538CrossRefGoogle ScholarPubMed
Yoshida, M., Banville, D. L. & Shafer, R. H. 1990 Structural analysis of d(GCAATTGC)2 and its complex with Berenil by nuclear magnetic resonance spectroscopy. Biochemistry 29 6585–6592CrossRefGoogle ScholarPubMed