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
. 1967 Sep;58(3):1126–1130. doi: 10.1073/pnas.58.3.1126

Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli.

F H Pettit, L J Reed
PMCID: PMC335757  PMID: 4964085

Full text

PDF

Images in this article

Selected References

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

  1. BEINERT H., PAGE E. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. V. Oxidation-reductions of the flavoproteins. J Biol Chem. 1957 Mar;225(1):479–497. [PubMed] [Google Scholar]
  2. Cline A. L., Bock R. M. Translational control of gene expression. Cold Spring Harb Symp Quant Biol. 1966;31:321–333. doi: 10.1101/sqb.1966.031.01.042. [DOI] [PubMed] [Google Scholar]
  3. GRABAR P., WILLIAMS C. A., Jr Méthode immuno-électrophorétique d'analyse de mélanges de substances antigéniques. Biochim Biophys Acta. 1955 May;17(1):67–74. doi: 10.1016/0006-3002(55)90320-6. [DOI] [PubMed] [Google Scholar]
  4. HENNING U., HERZ C. EIN STRUKTURGEN-KOMPLEX FUER DEN PYRUVAT-DEHYDROGENASE-KOMPLEX VON ESCHERICHIA COLI K 12. Z Vererbungsl. 1964 Nov 11;95:260–275. [PubMed] [Google Scholar]
  5. Henning U., Dennert G., Hertel R., Shipp W. S. Translation of the structural genes of the E. coli pyruvate dehydrogenase complex. Cold Spring Harb Symp Quant Biol. 1966;31:227–234. doi: 10.1101/sqb.1966.031.01.031. [DOI] [PubMed] [Google Scholar]
  6. KAPLAN S., ENSIGN S., BONNER D. M., MILLS S. E. GENE PRODUCTS OF CRM -- MUTANTS AT THE TD LOCUS. Proc Natl Acad Sci U S A. 1964 Mar;51:372–378. doi: 10.1073/pnas.51.3.372. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KOIKE M., REED L. J., CARROLL W. R. alpha-Keto acid dehydrogenation complexes. I. Purification and properties of pyruvate and alpha-ketoglutarate dehydrogenation complexes of Escherichia coli. J Biol Chem. 1960 Jul;235:1924–1930. [PubMed] [Google Scholar]
  8. KOIKE M., REED L. J., CARROLL W. R. alpha-Keto acid dehydrogenation complexes. IV. Resolution and reconstitution of the Escherichia coli pyruvate dehydrogenation complex. J Biol Chem. 1963 Jan;238:30–39. [PubMed] [Google Scholar]
  9. Kitto G. B., Wassarman P. M., Kaplan N. O. Enzymatically active conformers of mitochondrial malate dehydrogenase. Proc Natl Acad Sci U S A. 1966 Aug;56(2):578–585. doi: 10.1073/pnas.56.2.578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LEBOY P. S., COX E. C., FLAKS J. G. THE CHROMOSOMAL SITE SPECIFYING A RIBOSOMAL PROTEIN IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1964 Dec;52:1367–1374. doi: 10.1073/pnas.52.6.1367. [DOI] [PMC free article] [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. LUSTY C. J. LIPOYL DEHYDROGENASE FROM BEEF LIVER MITOCHONDRIA. J Biol Chem. 1963 Oct;238:3443–3452. [PubMed] [Google Scholar]
  13. MASSEY V., HOFMANN T., PALMER G. The relation of function and structure in lipoyl dehydrogenase. J Biol Chem. 1962 Dec;237:3820–3828. [PubMed] [Google Scholar]
  14. REICHLIN M., HAY M., LEVINE L. ANTIBODIES TO HUMAN A1 HEMOGLOBIN AND THEIR REACTION WITH A2, S, C, AND H HEMOGLOBINS. Immunochemistry. 1964 Apr;1:21–30. doi: 10.1016/0019-2791(64)90052-7. [DOI] [PubMed] [Google Scholar]
  15. Stein A. M., Stein J. H. Studies on the Straub diaphorase. I. Isolation of multiple forms. Biochemistry. 1965 Aug;4(8):1491–1500. doi: 10.1021/bi00884a005. [DOI] [PubMed] [Google Scholar]
  16. Stein A. M., Wolf B., Stein J. H. Studies on the Straub diaphorase. II. Properties of an antibody to the Straub diaphorase. Biochemistry. 1965 Aug;4(8):1500–1505. doi: 10.1021/bi00884a006. [DOI] [PubMed] [Google Scholar]
  17. WASSERMAN E., LEVINE L. Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition. J Immunol. 1961 Sep;87:290–295. [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