Skip to main content
PMC home page
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 Apr;47(4):551–566. doi: 10.1073/pnas.47.4.551

THE PROPERTIES OF ALTERED PROTEINS FROM MUTANTS BEARING ONE OR TWO LESIONS IN THE SAME GENE*

Barbara D Maling 1,†, Charles Yanofsky 1
PMCID: PMC221486  PMID: 13765795

Full text

PDF
554

Selected References

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

  1. ADELBERG E. A., MYERS J. W. Modification of the penicillin technique for the selection of auxotrophic bacteria. J Bacteriol. 1953 Mar;65(3):348–353. doi: 10.1128/jb.65.3.348-353.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Benzer S. ON THE TOPOLOGY OF THE GENETIC FINE STRUCTURE. Proc Natl Acad Sci U S A. 1959 Nov;45(11):1607–1620. doi: 10.1073/pnas.45.11.1607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Crawford I. P., Yanofsky C. ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS. Proc Natl Acad Sci U S A. 1958 Dec 15;44(12):1161–1170. doi: 10.1073/pnas.44.12.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crawford I. P., Yanofsky C. THE FORMATION OF A NEW ENZYMATICALLY ACTIVE PROTEIN AS A RESULT OF SUPPRESSION. Proc Natl Acad Sci U S A. 1959 Aug;45(8):1280–1287. doi: 10.1073/pnas.45.8.1280. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HUNT J. A., INGRAM V. M. Abnormal human haemoglobins. II. The chymotryptic digestion of the trypsin-resistant core of haemoglobins A and S. Biochim Biophys Acta. 1958 Jun;28(3):546–549. doi: 10.1016/0006-3002(58)90517-1. [DOI] [PubMed] [Google Scholar]
  6. INGRAM V. M. Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin. Nature. 1957 Aug 17;180(4581):326–328. doi: 10.1038/180326a0. [DOI] [PubMed] [Google Scholar]
  7. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. YANOFSKY C., RACHMELER M. The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim Biophys Acta. 1958 Jun;28(3):640–641. doi: 10.1016/0006-3002(58)90533-x. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Yanofsky C., Crawford I. P. THE EFFECTS OF DELETIONS, POINT MUTATIONS, REVERSIONS AND SUPPRESSOR MUTATIONS ON THE TWO COMPONENTS OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1959 Jul;45(7):1016–1026. doi: 10.1073/pnas.45.7.1016. [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]

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