Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1961 Sep;47(9):1440–1450. doi: 10.1073/pnas.47.9.1440

ENZYME COMPLEMENTATION IN MIXED EXTRACTS OF MUTANTS FROM THE SALMONELLA HISTIDINE B LOCUS*

John C Loper 1
PMCID: PMC223157  PMID: 13763426

Full text

PDF
1440

Images in this article

Selected References

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

  1. ADAMS E. L-Histidinal, a biosynthetic precursor of histidine. J Biol Chem. 1955 Nov;217(1):325–344. [PubMed] [Google Scholar]
  2. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  3. AMES B. N., HORECKER B. L. The biosynthesis of histidine: imidazoleacetol phosphate transaminase. J Biol Chem. 1956 May;220(1):113–128. [PubMed] [Google Scholar]
  4. AMES B. N., MITCHELL H. K. The biosynthesis of histidine; imidazoleglycerol phosphate, imidazoleacetol phosphate, and histidinol phosphate. J Biol Chem. 1955 Feb;212(2):687–696. [PubMed] [Google Scholar]
  5. AMES B. N. The biosynthesis of histidine; D-erythro-imidazoleglycerol phosphate dehydrase. J Biol Chem. 1957 Sep;228(1):131–143. [PubMed] [Google Scholar]
  6. AMES B. N. The biosynthesis of histidine; L-histidinol phosphate phosphatase. J Biol Chem. 1957 Jun;226(2):583–593. [PubMed] [Google Scholar]
  7. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. COHN M. I. Production of antibodies in experimental animals. Methods Med Res. 1952;5:271–283. [PubMed] [Google Scholar]
  9. FINCHAM J. R. Genetically controlled differences in enzyme activity. Adv Enzymol Relat Subj Biochem. 1960;22:1–43. doi: 10.1002/9780470122679.ch1. [DOI] [PubMed] [Google Scholar]
  10. HARTMAN P. E., LOPER J. C., SERMAN D. Fine structure mapping by complete transduction between histidine-requiring Salmonella mutants. J Gen Microbiol. 1960 Apr;22:323–353. doi: 10.1099/00221287-22-2-323. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  13. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  14. WOODWARD D. O. A gene concept based on genetic and chemical studies in neurospora. Q Rev Biol. 1960 Dec;35:313–323. doi: 10.1086/403190. [DOI] [PubMed] [Google Scholar]
  15. Woodward D. O. ENZYME COMPLEMENTATION IN VITRO BETWEEN ADENYLOSUCCINASELESS MUTANTS OF NEUROSPORA CRASSA. Proc Natl Acad Sci U S A. 1959 Jun;45(6):846–850. doi: 10.1073/pnas.45.6.846. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. YANOFSKY C. The tryptophan synthetase system. Bacteriol Rev. 1960 Jun;24(2):221–245. doi: 10.1128/br.24.2.221-245.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES