Abstract
Summary
Chromatography of rat kidney lysozyme with Amberlite XE-64 ion-exchange resin by direct and gradient elution procedures have been described. Three peaks of enzyme activity have been resolved by either procedure. Separate rechromatography of each peak by direct elution substantiated that none of the peaks was an artifact. The central peak contains the major portion of enzyme activity and after rechromatography the enzyme is spectrophotometrically free of cytochrome c. Cytochrome c appeared, after direct elution, as 4 peaks closely associated with the enzyme due to similar physical-chemical properties. Two peaks of reduced and oxidized cytochrome were found by gradient elution. Total purification of the specific enzyme activity was about 100-fold over the original supernatant.
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