Abstract
A protein exhibiting immunological cross-reactivity with NADP-specific isocitrate dehydrogenase, but containing no catalytic activity, has been isolated from nalidixic acid-resistantEscherichia coli. The two proteins have, within the limits of experimentation, identical molecular weight, subunit structure, and amino acid homology. The absence of catalytic activity in the protein isolated from nalidixic acid-resistant mutants may result from a mutation in the isocitrate dehydrogenase structural gene.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature Cited
Andrews, P. 1964. Estimation of molecular weights of proteins by Sephadex gel filtration. Biochemical Journal91:222–233.
Apostolakos, D., Menter, P. A., Reeves, H. C., Birge, E. A. 1979. Location of the structural gene for isocitrate dehydrogenase ofEscherichia coli K-12. Genetics92:s2.
Garnak, M., Reeves, H. C. 1979. Phosphorylation of isocitrate dehydrogenase ofEscherichia coli. Science203:1111–1112.
Garnak, M., Reeves, H. C.. 1979. Purification and properties of phosphorylated isocitrate dehydrogenase ofEscherichia coli. Journal of Biological Chemistry254:7915–7920.
Helling, R. B., Kukora, J. S. 1971. Nalidixic acid-resistant mutants ofEscherichia coli deficient in isocitrate dehydrogenase. Journal of Bacteriology105:1224–1226.
Laurell, C. B. 1966. Quantitative estimation of proteins by electrophoresis in antibody-containing agarose gel. Analytical Biochemistry15:45–52.
Marchalonis, J. J., Weltman, J. K. 1971. Relatedness among proteins: A new method of estimation and its application to immunoglobins. Comparative Biochemistry and Physiology38B:609–625.
Menter, P.A. 1979. Purification and properties of inactive NADP-isocitrate dehydrogenase from NalR Escherichia coli. Master's thesis. Arizona State University, Tempe, Arizona.
Rampsch, B. J., Birge, E. A. 1975. Mutations associated with nalidixic acid resistance and their relationship to antibiotic resistance mutations affecting fidelity of translation inEscherichia coli KL-98 Genetics80:s66.
Reeves, H. C., Burke, W. F., Jr. 1974. Molecular weight ofEscherichia coli NADP-isocitrate dehydrogenase. Biochimica et Biophysica Acta366:396–398.
Reeves, H. C., Daumy, G. O., Lin, C. C., Houston, M. 1972. NADP-specific isocitrate dehydrogenase ofEscherichia coli. I. Purification and characterization. Biochimica et Biophysica Acta258:27–39.
Spackman, D. H., Stein, W. H., Moore, S. 1958. Automatic recording apparatus for use in the chromatography of amino acids. Analytical Biochemistry30:1190–1199.
Vasquez, B., Reeves, H. C. 1979. NADP-specific isocitrate dehydrogenase ofEscherichia coli. IV. Purification by chromatography on Affi-Gel blue. Biochimica et Biophysica Acta579:31–40.
Weber, K., Osborn, M. 1969. The reliability of molecular weight determinations by dodecyl sulfate polyacrylamide gel electrophoresis. Journal of Biological Chemistry244:4406–4412.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Menter, P.A., Reeves, H.C. A catalytically inactive form of isocitrate dehydrogenase fromEscherichia coli . Current Microbiology 5, 353–355 (1981). https://doi.org/10.1007/BF01566748
Issue Date:
DOI: https://doi.org/10.1007/BF01566748