Adenylate Kinase from Pseudomonas denitrificans

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Abstract
1. Adenylate kinase [EC 2.7.4.3] has been purified approximately 200-fold from Pseudomonas denitrificans. The purified enzyme was nearly homogenous on polyacryl-amide gel disc electrophoresis. 2. The molecular weight of the enzyme was estimated to be 21,000 by the gel-filtration method. The heat stability, Km value and sensitivity to SH-inhibitors were compared with those of enzyme purified from other sources. 3. Antiserum against purified enzyme has been prepared from immunized rabbit. This antiserum inhibited 100 percent of the enzyme activity. Ouchterlony double diffusion tests showed one major and a few minor precipitin bands between the purified enzyme and the antiserum. 4. Immunological similarities of adenylate kinases from various sources were examined by comparing the degrees of inhibition of the activities by the antiserum.

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