Immunochemical studies on acetylornithine 5-aminotransferase from Pseudomonas aeruginosa |
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| Authors: | R. Voellmy R. Utzinger |
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| Affiliation: | (1) Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, CH-8000 Zürich, (Switzerland);(2) Present address: Dept. of Physiology, Harvard Medical School, 25 Shattuck Street, 02115 Boston, Mass., USA;(3) Institute of Toxicology, Swiss Federal Institute of Technology, CH-8603 Schwerzenbach, Switzerland |
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| Abstract: | Summary Mouse antibodies with specificity towards acetylornithine 5-aminotransferase (ACOAT) from Pseudomonas aeruginosa were used to study the structural similarities of serveral 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.Acknowledgment. We wish to thank Prof. J. Lindenmann for helpful discussions. |
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