A New Kinetic Method for Analysing the Parameters of Immobilized Aldolase
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.
KeywordsFeed Rate Immobilize Enzyme Democratic Republic Kinetic Mechanism Hungarian Academy
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