Hostname: page-component-78c5997874-g7gxr Total loading time: 0 Render date: 2024-11-02T20:03:14.891Z Has data issue: false hasContentIssue false
  • English
  • Français

The antimicrobial activity of cationic proteins isolated from the cells in bulk milk samples

Published online by Cambridge University Press:  15 May 2009

K. G. Hibbitt ,
J. Brownlie  and
C. B. Cole
K. G. Hibbitt
Affiliation:
Institute for Research on Animal Diseases, Compton, Newbury, Berkshire
J. Brownlie
Affiliation:
Institute for Research on Animal Diseases, Compton, Newbury, Berkshire
C. B. Cole
Affiliation:
Institute for Research on Animal Diseases, Compton, Newbury, Berkshire
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Cationic proteins isolated from the cells in bulk milk samples were shown to inhibit the growth of two pathogenic strains of staphylococci and also Streptococcus agalactiae S 13. Polyacrylamide gel disk electrophoresis studies on these proteins revealed the presence of at least 9 components some of which had isoelectric pH's between 7·0 and 9·0. Trace amounts of the isolated protein had isoelectric pH's greater than 9·0. Staphylococci incubated with milk-cell cationic proteins absorbed the protein, thereby allowing the organism to be stained with the anionic dye Fast Green FCF. Protein-treated staphylococci in isotonic solutions autoagglutinated. This autoagglutination was more marked in hypo- and hypertonic solutions. Lysozyme was not demonstrated in the isolated protein fractions in assays involving incubation with Micrococcus lysodeikticus for 90 min. The antimicrobial activity of the cationic proteins isolated from the bulk milk samples was not destroyed after heating to temperatures up to 70° C for 30 min., whereas at higher temperatures the activity diminished and was almost completely lost at 100° C.

Type
Research Article
Information
Journal of Hygiene , Volume 69 , Issue 1 , March 1971 , pp. 61 - 68
Copyright
Copyright © Cambridge University Press 1971

References

REFERENCES

Blackburn, P. S., Laing, C. M. & Malcolm, D. F. (1955). A comparison of the diagnostic value of the total and differential cell counts of bovine milk. Journal of Dairy Research 22, 37–42.CrossRefGoogle Scholar
Blobel, H. & Katsube, Y. (1964). Effects of experimentally induced leucocytosis in bovine mammary gland upon infections with Staphylococcus aureus, Streptococcus agalactiae, and Aerobacter aerogenes. American Journal of Veterinary Research 25, 1085–9.Google ScholarPubMed
Bloom, W. L. & Blake, F. G. (1948). Studies on an antibacterial polypeptide extracted from normal tissues. Journal of Infectious Diseases 83, 116–23.CrossRefGoogle Scholar
Bloom, W. L., Winters, M. G. & Watson, D. W. (1951). The inhibition of two antibacterial basic proteins by nucleic acids. Journal of Bacteriology 62, 7–13.CrossRefGoogle ScholarPubMed
Derbyshire, J. B. (1964). The multiplication of Staphylococcus aureus in the milk of cows with mild mastitis. Journal of Pathology and Bacteriology 87, 137–44.CrossRefGoogle ScholarPubMed
Dilbat, K. (1963). Inaug. Diss., Tierärztliche Hochschule, Hannover, p. 43.Google Scholar
Dubos, R. J. (1945). The Bacterial Cell, chap. 6. Cambridge, Mass.: Harvard University Press.Google Scholar
Fevold, H. L. (1951). Egg proteins. Advances in Protein Chemistry 6, 187–252.CrossRefGoogle ScholarPubMed
Hibbitt, K. G. & Cole, C. B. (1968). The antimicrobial activity of teat canal cationic proteins. Biochemical Journal 106, 39 P.Google Scholar
Hibbitt, K. B., Cole, C. B. & Reiter, B. (1969). Antimicrobial proteins isolated from the teat canal of the cow. Journal of General Microbiology 56, 365–71.CrossRefGoogle ScholarPubMed
Jain, N. C. & Jasper, D. E. (1967). Phagocytosis and destruction of Aerobacter aerogenes by leukocytes from bovine milk. American Journal of Veterinary Research 28, 405–11.Google ScholarPubMed
Katsube, Y. & Blobel, H. (1964). In vitro phagocytic activities of leukocytes isolated from the mammary secretions of a cow. American Journal of Veterinary Research 25, 1090–95.Google ScholarPubMed
Padgett, G. A. & Hirsch, J. G. (1967). Lysozyme: its absence in tears and leukocytes of cattle. Australian Journal of Experimental Biology and Medical Science 45, 569–70.CrossRefGoogle ScholarPubMed
Parry, R. M., Chandon, R. C. & Shahani, K. M. (1964). Purification of milk lysozyme. Journal of Dairy Science 47, 663.Google Scholar
Schalm, O. W., Lasmanis, J. & Carroll, E. J. (1964 a). Pathogenesis of experimental coliform (Aerobacter aerogenes) mastitis in cattle. American Journal of Veterinary Research 25, 75–82.Google ScholarPubMed
Schalm, O. W., Lasmanis, J. & Carboll, E. J. (1964 b). Effects of pre-existing leukocytosis on experimental coliform (Aerobacter aerogenes) mastitis in cattle. American Journal of Veterinary Research 25, 83–9.Google ScholarPubMed
Shugar, D. (1952). The measurement of lysozyme activity and the ultraviolet inactivation of lysozyme. Biochimica et biophysica acta 8, 302–9.CrossRefGoogle ScholarPubMed
Skarnes, R. C. & Watson, D. W. (1956). Characterization of leukin: an antibacterial factor from leucocytes active against Gram-positive pathogens. Journal of Experimental Medicine 104, 829–45.CrossRefGoogle ScholarPubMed
Zeya, H. I. & Spitznagel, J. K. (1966). Cationic proteins of polymorphonuclear leukocyte lysosomes. Journal of Bacteriology 91, 755–62.CrossRefGoogle ScholarPubMed
Zlotnik, I. (1947). Types of cells present in cow's milk. Journal of Comparative Pathology 57, 196–208.CrossRefGoogle ScholarPubMed