This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Steele, W. F.
Right arrow Articles by Morrison, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steele, W. F.
Right arrow Articles by Morrison, M.

 Previous Article  |  Next Article 

J Bacteriol. 1969 February; 97(2): 635-639
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Antistreptococcal Activity of Lactoperoxidase

Wilbert F. Steele1 and Martin Morrison2

a Department of Biochemistry, City of Hope Medical Center, Duarte, California 91010

ABSTRACT

A study of the inhibition of the growth of Streptococcus cremoris 972 by the enzyme lactoperoxidase has shown, in agreement with previous investigations, that the inhibition requires a source of both peroxide and thiocyanate. The thiocyanate may play more than one role. It stabilizes the very dilute solutions of lactoperoxidase employed in these studies, and its oxidation products may be involved in the inhibition. Binding of the enzyme by the microorganism is suggested by the fact that when the organism was preincubated with the enzyme and then in a medium free from the enzyme, but containing peroxide and thiocyanate, the growth of the organism was inhibited. This inhibition has all the properties of the enzyme-containing system. Although no dialyzable factor could be demonstrated to cause the inhibition, the inhibitory state involving peroxide, the enzyme, and thiocyanate survived for at least 60 min before cells were added to the medium. When catalase was present in the medium prior to the addition of the cells, the inhibition was completely reversed. It was only partially reversed if catalase was added a few moments after the addition of the cells. The data have been interpreted as indicating that the inhibition takes place rapidly and requires the formation of a quaternary complex of the cells, thiocyanate, peroxide, and the enzyme lactoperoxidase.

FOOTNOTES

1 Present address: Department of Biochemistry and Biophysics Oregon State University, Corvallis, Ore. 97331.

2 Present address: Department of Biochemistry, St. Jude Children's Research Hospital, and University of Tennessee Medical Units, Memphis, Tenn. 38101.

J Bacteriol. 1969 February; 97(2): 635-639
Copyright © 1969 American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lonnerdal, B. (2003). Nutritional and physiologic significance of human milk proteins. Am. J. Clin. Nutr. 77 : 1537S-1543S [Abstract] [Full Text]  
  • Scannapieco, F. A. (1994). Saliva-Bacterium Interactions in Oral Microbial Ecology. CROBM 5: 203-248 [Abstract] [Full Text]  
  • Thomas, E.L., Bates, K.P., Jefferson, M.M. (1981). Peroxidase Antimicrobial System of Human Saliva: Requirements for Accumulation of Hypothiocyanite. JDR 60: 785-796 [Abstract]  
  • Thomas, E. L., Pera Bates, K., Jefferson, M. M. (1980). Hypothiocyanite Ion: Detection of the Antimicrobial Agent in Human Saliva. JDR 59: 1466-1472 [Abstract]  
  • Mandel, I. D. (1976). Nonimmunologic Aspects of Caries Resistance. JDR 55: C22-C31  
  • Iwamoto, Y., Nakamura, R., Watanabe, T., Tsunemitsu, A. (1972). Heterogeneity of Peroxidase Related to Antibacterial Activity in Human Parotid Saliva. JDR 51: 503-508 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»