1887

Abstract

SUMMARY: Antisera to the penicillinases of strains 749 and 6346 were prepared, and the neutralization of enzymic activity by homologous and heterologous antisera was studied. Antisera to 749 penicillinase had, as expected, greater neutralizing power against 749 penicillinase than against 6346 penicillinase. A 6346 antiserum, however, neutralized the heterologous enzyme more effectively than the homologous enzyme, and was also more effective in precipitating heterologous than homologous enzymic activity. The penicillinases of , unlike those of , could not be adsorbed on glass, but could be partially purified by calcium phosphate gel-adsorption. There was no cross-reaction, as measured by enzyme neutralization, between the penicillinases of and that of 569. Materials other than penicillinase in the enzyme preparations used did not interfere with the neutralization reactions between penicillinases and their antisera. The basal penicillinase produced by 749 had the same neutralization curve, with a homologous antiserum, as did the induced enzyme.

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/content/journal/micro/10.1099/00221287-23-2-381
1960-10-01
2021-10-16
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References

  1. Boyd W. C. 1956 Fundamentals of Immunology, 3rd ed.. New York: Interscience Publishers Inc;
    [Google Scholar]
  2. Brown G. L. 1952; A solubility analysis of crystalline ox-liver catalase. Biochem. J 51:569
    [Google Scholar]
  3. Cinader B. 1957; Antibodies against enzymes. Annu. Rev. Microbiol 11:371
    [Google Scholar]
  4. Craig L. C., Gregory J. D., Hausmann W. 1950; Versatile laboratory concentration device. Anal. Chem 22:1462
    [Google Scholar]
  5. Dixon M., Webb E. C. 1958 Enzymes London: Longmans, Green and Co;
    [Google Scholar]
  6. Freund J., McDermott K. 1942; Sensitization to horse serum by means of adjuvants. Proc. Soc. exp. Biol., N.Y 49548
    [Google Scholar]
  7. Henry R. J., Housewright R. D. 1947; Studies in penicillinase. II. Manometric method of assaying penicillinase and penicillin, kinetics of the penicillin-penicillinase reaction and the effect of inhibitors on penicillinase. J. biol. Chem 167:559
    [Google Scholar]
  8. Keilin D., Hartree E. F. 1938; On the mechanism of the decomposition of hydrogen peroxide by catalase. Proc. roy. Soc B 124:397
    [Google Scholar]
  9. Kogut M., Pollock M. R., Tridgell E. J. 1956; Purification of penicillin-induced penicillinase of Bacillus cereus NRRL 569: a comparison of its properties with those of a similarly purified penicillinase produced spontaneously by a constitutive mutant strain. Biochem. J 62:391
    [Google Scholar]
  10. Neilands J. B. 1952; Studies on lactic dehydrogenase of heart I. Purity, kinetics and equilibria. J. biol. Chem 199:373
    [Google Scholar]
  11. Pollock M. R. 1950; Penicillinase adaptation in B. cereus: Adaptive enzyme formation in the absence of free substrate. Brit. J. exp. Path 31:739
    [Google Scholar]
  12. Pollock M. R. 1956a; An immunological study of the constitutive and penicillin-induced penicillinases of Bacillus cereus, based on specific enzyme neutralization by antibody. J. gen. Microbiol 14:90
    [Google Scholar]
  13. Pollock M. R. 1956b; The cell-bound penicillinase of Bacillus cereus . J. gen. Microbiol 15:154
    [Google Scholar]
  14. Pollock M. R. 1961; Exo-enzymes. In The Bacteria 4 Gunsalus I. C., Stanier R. Y. ed. New York: Academic Press Inc.;
    [Google Scholar]
  15. Pollock M. R., Kramer M. 1958; Intermediates in the biosynthesis of bacterial penicillinase. Biochem. J 70:665
    [Google Scholar]
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