Comparison of Dihydrofolate Reductases Obtained from Trimethoprim and Sulfonamide Resistance of (Neisseria Gonorrhoeae).

Abstract

Dihydrofolate reductases from two strains (CDC 9 and 7134) of Neisseria gonorrhoeae with different sensitivity to sulfamethoxazole (60 fold) and trimethoprim (2 fold) have been isolated and purified. The reductases are strikingly similar in most respects. Purification steps produced essentially similar results with both enzymes. The pH profiles of both reductases were virtually identical; and the effect of increasing salt concentration was the same. There were no significant differences in any of the kinetic parameters. The enzymes do differ with respect to thermostability, substrate protection against heat inactivation and the ir response to inhibition by methotrexate.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 1977
Accession Number
ADA052725

Entities

People

  • Leonard Corman
  • Richard I. Ho

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amides
  • Amino Acids
  • Biological Pigments
  • Birds
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Chromatography
  • Column Chromatography
  • Cysteine
  • Gel Electrophoresis
  • Inhibition
  • Inhibitors
  • Molecular Weight
  • Molecules
  • Reducing Agents
  • Resistance

Fields of Study

  • Biology

Readers

  • Microbial Pathology
  • Thermal Physics or Thermal Science.