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
. 1965 Oct;54(4):1174–1181. doi: 10.1073/pnas.54.4.1174

Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli.

E Steers Jr, G R Craven, C B Anfinsen
PMCID: PMC219826  PMID: 5327255

Full text

PDF
1174

Images in this article

Selected References

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

  1. BALBINDER E., PREER J. R., Jr Gel diffusion studies on serotype and serotype transformation in Paramecium. J Gen Microbiol. 1959 Aug;21:156–167. doi: 10.1099/00221287-21-1-156. [DOI] [PubMed] [Google Scholar]
  2. BEAVEN G. H., HOLIDAY E. R. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. doi: 10.1016/s0065-3233(08)60022-4. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. CRAVEN G. R., STEERS E., Jr, ANFINSEN C. B. PURIFICATION, COMPOSITION, AND MOLECULAR WEIGHT OF THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2468–2477. [PubMed] [Google Scholar]
  5. GROSS E., WITKOP B. Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1856–1860. [PubMed] [Google Scholar]
  6. 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]
  7. KATZ A. M., DREYER W. J., ANFINSEN C. B. Peptide separation by two-dimensional chromatography and electrophoresis. J Biol Chem. 1959 Nov;234:2897–2900. [PubMed] [Google Scholar]
  8. MILLER G. L., GOLDER R. H. Buffers of pH 2 to 12 for use in electrophoresis. Arch Biochem. 1950 Dec;29(2):420–423. [PubMed] [Google Scholar]
  9. PREER J. R., Jr A quantitative study of a technique of double diffusion in agar. J Immunol. 1956 Jul;77(1):52–60. [PubMed] [Google Scholar]
  10. REDFIELD R. R., ANFINSEN C. B. The structure of ribonuclease. II. The preparation, separation, and relative alignment of large enzymatically produced fragments. J Biol Chem. 1956 Jul;221(1):385–404. [PubMed] [Google Scholar]
  11. STEERS E., Jr, CRAVEN G. R., ANFINSEN C. B., BETHUNE J. L. EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2478–2484. [PubMed] [Google Scholar]
  12. Sanger F. The free amino groups of insulin. Biochem J. 1945;39(5):507–515. doi: 10.1042/bj0390507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. YANOFSKY C., CARLTON B. C., GUEST J. R., HELINSKI D. R., HENNING U. ON THE COLINEARITY OF GENE STRUCTURE AND PROTEIN STRUCTURE. Proc Natl Acad Sci U S A. 1964 Feb;51:266–272. doi: 10.1073/pnas.51.2.266. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]
  15. ZIPSER D. A STUDY OF THE UREA-PRODUCED SUBUNITS OF BETA-GALACTOSIDASE. J Mol Biol. 1963 Aug;7:113–121. doi: 10.1016/s0022-2836(63)80040-6. [DOI] [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