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
. 1968 Aug;60(4):1260–1267. doi: 10.1073/pnas.60.4.1260

Genetic evidence for the disposition of the substrate binding site of beta-galactosidase.

J Langridge
PMCID: PMC224912  PMID: 4877266

Full text

PDF
1260

Selected References

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

  1. BECKWITH J. R. A DELETION ANALYSIS OF THE LAC OPERATOR REGION IN ESCHERICHIA COLI. J Mol Biol. 1964 Mar;8:427–430. doi: 10.1016/s0022-2836(64)80206-0. [DOI] [PubMed] [Google Scholar]
  2. DIXON M. The determination of enzyme inhibitor constants. Biochem J. 1953 Aug;55(1):170–171. doi: 10.1042/bj0550170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fowler A. V., Zabin I. Co-linearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains. Science. 1966 Nov 25;154(3752):1027–1029. doi: 10.1126/science.154.3752.1027. [DOI] [PubMed] [Google Scholar]
  4. HORIUCHI T., TOMIZAWA J. I., NOVICK A. Isolation and properties of bacteria capable of high rates of beta-galactosidase synthesis. Biochim Biophys Acta. 1962 Jan 22;55:152–163. doi: 10.1016/0006-3002(62)90941-1. [DOI] [PubMed] [Google Scholar]
  5. JACOB F., ULLMAN A., MONOD J. LE PROMOTEUR, 'EL'EMENT G'EN'ETIQUE N'ECESSAIRE 'A L'EXPRESSION D'UN OP'ERON. C R Hebd Seances Acad Sci. 1964 Mar 16;258:3125–3128. [PubMed] [Google Scholar]
  6. Johnson L. N., Phillips D. C. Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6 Angstrom resolution. Nature. 1965 May 22;206(4986):761–763. doi: 10.1038/206761a0. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. MUELLER-HILL B., RICKENBERG H. V., WALLENFELS K. SPECIFICITY OF THE INDUCTION OF THE ENZYMES OF THE LAC OPERON IN ESCHERICHIA COLI. J Mol Biol. 1964 Nov;10:303–318. doi: 10.1016/s0022-2836(64)80049-8. [DOI] [PubMed] [Google Scholar]
  9. Newton W. A., Beckwith J. R., Zipser D., Brenner S. Nonsense mutants and polarity in the lac operon of Escherichia coli. J Mol Biol. 1965 Nov;14(1):290–296. doi: 10.1016/s0022-2836(65)80250-9. [DOI] [PubMed] [Google Scholar]
  10. PERRIN D. Immunological studies with genetically altered beta-galactosidases. Ann N Y Acad Sci. 1963 May 8;103:1058–1066. doi: 10.1111/j.1749-6632.1963.tb53757.x. [DOI] [PubMed] [Google Scholar]
  11. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yanofsky C., Stadler J. THE ENZYMATIC ACTIVITY ASSOCIATED WITH THE PROTEIN IMMUNOLOGICALLY RELATED TO TRYPTOPHAN SYNTHETASE. Proc Natl Acad Sci U S A. 1958 Mar;44(3):245–253. doi: 10.1073/pnas.44.3.245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. ZAMENHOF S. Gene unstabilization induced by heat and by nitrous acid. J Bacteriol. 1961 Jan;81:111–117. doi: 10.1128/jb.81.1.111-117.1961. [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