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Purification of Dehydrogenases and Kinases by Affinity Chromatography

  • C.-Y. Lee
  • L. H. Lazarus
  • N. O. Kaplan

Abstract

The concept of using adenine nucleotide derivatives as general ligands in affinity chromatography was first proposed by Mosbach and his coworkers (1-3). Various immobilized adenine nucleotide derivatives have been prepared and used in the selective purification of enzymes by means of general ligand affinity chromatography (11, 17–21). From the efforts of many workers it is apparent that further development of this methodology would greatly accelerate our understanding of enzymes and their utilization in biochemical research, clinical chemistry and industrial production. Selective purification of enzymes by general ligand affinity chromatography is based on the principle that a single immobilized general ligand has the capacity to adsorb a large number of enzymes, or a given family of enzymes, which either require the same cofactor or have a common inhibitor or activator.

Keywords

Creatine Kinase Lactate Dehydrogenase Pyruvate Kinase Malate Dehydrogenase Affinity Column 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1978

Authors and Affiliations

  • C.-Y. Lee
    • 1
  • L. H. Lazarus
    • 1
  • N. O. Kaplan
    • 1
  1. 1.Department of ChemistryUniversity of California, San DiegoLa JollaUSA

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