Literature DB >> 408176

Immunochemical studies on acetylornithine 5-aminotransferase from Pseudomonas aeruginosa.

R Voellmy, R Utzinger.   

Abstract

Mouse antibodies with specificity towards acetylornithine 5-aminotransferase (ACOAT) from Pseudomonas aeruginosa were used to study the structural similarities of several isofunctional enzymes from different sources. With the antibody directed against ACOAT, the amounts of enzyme present in cells grown under different conditions were determined. These experiments established that the enzyme is induced by arginine and is subject to repression by carbon sources.

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Year:  1977        PMID： 408176     DOI： 10.1007/bf01945932

Source DB:  PubMed          Journal:  Experientia        ISSN： 0014-4754


  5 in total

1.  Diffusion-in-gel methods for immunological analysis.

Authors:  O OUCHTERLONY
Journal:  Prog Allergy       Date:  1958

2.  Immunological studies on the key enzyme of arginine biosynthesis in Pseudomonas aeruginosa.

Authors:  R Utzinger
Journal:  Experientia       Date:  1977-08-15

3.  Inducible and repressible acetylornithine delta-transaminase in Escherichia coli: different proteins.

Authors:  J T Billheimer; E E Jones
Journal:  Arch Biochem Biophys       Date:  1974-04-02       Impact factor: 4.013

4.  Immunochemical quantitation of antigens by single radial immunodiffusion.

Authors:  G Mancini; A O Carbonara; J F Heremans
Journal:  Immunochemistry       Date:  1965-09

5.  Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism.

Authors:  R Voellmy; T Leisinger
Journal:  J Bacteriol       Date:  1975-06       Impact factor: 3.490
  5 in total
  1 in total

1.  Immunological studies on the key enzyme of arginine biosynthesis in Pseudomonas aeruginosa.

Authors:  R Utzinger
Journal:  Experientia       Date:  1977-08-15
  1 in total

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