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A New Kinetic Method for Analysing the Parameters of Immobilized Aldolase

  • Veronika Jancsik
  • Ferenc Bartha
  • Jurgen Lasch

Abstract

Rabbit muscle aldolase was attached to Sepharose 6B by CNBr activation. Under optimal conditions the yield was 70–90% for protein, but only 20–50% for enzyme activity, as measured immediately after coupling. This activity decreased to about 5% during a few days storage at +5°C, and then remained stable for some weeks. From initial velocity measurements we calculated the KMapp value, which did not significantly differ from the KM of the soluble enzyme.

Keywords

Feed Rate Immobilize Enzyme Democratic Republic Kinetic Mechanism Hungarian Academy 
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

© Plenum Press, New York 1978

Authors and Affiliations

  • Veronika Jancsik
    • 1
  • Ferenc Bartha
    • 1
  • Jurgen Lasch
    • 2
  1. 1.Institute of BiochemistryHungarian Academy ScienceBudapestHungary
  2. 2.Institute of Physiological ChemistryMartin Luther University, HalleSaaleGerman Democratic Republic

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