Adenylate kinase from rat liver: Molecular properties and structural comparison with yeast enzyme.

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  • ラット肝臓アデニレートキナーゼの分子性状および酵母酵素との比較
  • ラット肝臓アデニレートキナーゼの分子性状および酵母酵素との比較〔英文〕
  • ラット カンゾウ アデニレート キナーゼ ノ ブンシ セイジョウ オヨビ コウ

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Abstract

Adenylate kinase from rat liver was found to have a molecular weight in the range between 25000 and 33000 by sodium dodecylsulfate (SDS) polyacrylamide gel electrophoresis using the continuous and discontinuous buffer systems, sedimentation equilibrium, and Sephadex G-100 gel filtration. The purified enzyme was separated into three peaks of activities with isoelectric points (pl) of 8.1, 7.5, and 6.7, respectively, by column isoelectric focusing, and this heterogeneity may be due to deamidation. The purified enzyme had one disulfide bond which related to the active conformation of the enzyme and two sulfhydryl groups which did not contribute to the enzyme activity. Antibody against the purified rat liver adenylate kinase showed a cross-reactivity with yeast adenylate kinase, but antibody against the rat muscle isoenzyme showed no cross-reactivity with the yeast enzyme. On the other hand, antibody against the yeast enzyme cross-reacted with the rat liver isoenzyme but not with the rat muscle isoenzyme. These results indicate that there is a structural resemblance between the rat liver and yeast enzymes.

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