Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1956 Mar;62(3):391–403. doi: 10.1042/bj0620391

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

Margot Kogut 1,*, M R Pollock 1, E J Tridgell 1
PMCID: PMC1215928  PMID: 13303986

Full text

PDF
391

Images in this article

395Fig. 1.
on p.395

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BAUDET P., HAGEMANN G. Purification de la pénicillinase de Bacillus cereus. Experientia. 1954 Sep 15;10(9):374–376. doi: 10.1007/BF02160547. [DOI] [PubMed] [Google Scholar]
  2. Cecil R., Ogston A. G. The accuracy of the Svedberg oil-turbine ultracentrifuge. Biochem J. 1948;43(4):592–598. doi: 10.1042/bj0430592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GORINI L., FROMAGEOT C. Les facteurs physiologiques conditionnant la présence de protéinase dans les cultures de Micrococcus lysodeikticus. Biochim Biophys Acta. 1950 Jun;5(3/4):524–534. doi: 10.1016/0006-3002(50)90198-3. [DOI] [PubMed] [Google Scholar]
  4. HALL J. R., OGSTON A. G. Sedimentation and diffusion of samples of penicillinase. Biochem J. 1956 Mar;62(3):401–403. [PubMed] [Google Scholar]
  5. ITANO H. A. Human hemoglobin. Science. 1953 Jan 30;117(3031):89–94. doi: 10.1126/science.117.3031.89. [DOI] [PubMed] [Google Scholar]
  6. KANTOROWICZ O. An antibiotic assay tray. J Gen Microbiol. 1951 May;5(2):357–359. doi: 10.1099/00221287-5-2-357. [DOI] [PubMed] [Google Scholar]
  7. LANDMAN O. E. Neurospora lactase. II. Enzyme formation in the standard strain. Arch Biochem Biophys. 1954 Sep;52(1):93–109. doi: 10.1016/0003-9861(54)90092-2. [DOI] [PubMed] [Google Scholar]
  8. LEDERBERG J., LEDERBERG E. M. Replica plating and indirect selection of bacterial mutants. J Bacteriol. 1952 Mar;63(3):399–406. doi: 10.1128/jb.63.3.399-406.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  10. MANSON E. E., POLLOCK M. R., TRIDGELL E. J. A comparison of the properties of penicillinase produced by Bacillus subtilis and Bacillus cereus with and without addition of penicillin. J Gen Microbiol. 1954 Dec;11(3):493–505. doi: 10.1099/00221287-11-3-493. [DOI] [PubMed] [Google Scholar]
  11. MONOD J., COHN M. La biosynthèse induite des enzymes; adaptation enzymatique. Adv Enzymol Relat Subj Biochem. 1952;13:67–119. [PubMed] [Google Scholar]
  12. POLLOCK M. R. An immunological study of the constitutive and the penicillin-induced penicillinases of Bacillus cereus, based on specific enzyme neutralization by antibody. J Gen Microbiol. 1956 Feb;14(1):90–108. doi: 10.1099/00221287-14-1-90. [DOI] [PubMed] [Google Scholar]
  13. POLLOCK M. R., PERRET C. J. The relation between fixation of penicillin sulphur and penicillinase adaptation in B cereus. Br J Exp Pathol. 1951 Oct;32(5):387–396. [PMC free article] [PubMed] [Google Scholar]
  14. POLLOCK M. R. Penicillinase adaptation in B. cereus; adaptive enzyme formation in the absence of free substrate. Br J Exp Pathol. 1950 Dec;31(6):739–753. [PMC free article] [PubMed] [Google Scholar]
  15. POLLOCK M. R., TORRIANI A. M. Purification et caractéristiques physicochimiques de la pénicillinase de Bacillus cereus. C R Hebd Seances Acad Sci. 1953 Jul 20;237(3):276–278. [PubMed] [Google Scholar]
  16. POLLOCK M. R., TORRIANI A. M., TRIDGELL E. J. Crystalline bacterial penicillinase. Biochem J. 1956 Mar;62(3):387–391. doi: 10.1042/bj0620387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. SNEATH P. H. Proof of the spontaneity of a mutation to penicillinase production in Bacillus cereus. J Gen Microbiol. 1955 Dec;13(3):561–568. doi: 10.1099/00221287-13-3-561. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES