Abstract
Summary
Active cross-linked derivatives of egg-white lysozyme have been prepared by reaction with 4,4′-difluoro-3,3′-dinitrophenyl-sulfone and isolated from excess reagents and salts by gel chromatography. Lytic activity of the enzyme at pH 9.21 is almost abolished in one cross-linked derivative which still retains 20% of its lytic activity at pH 6.24. The potential importance of such cross-linked enzymes is discussed in connection with stabilization of enzyme structure towards inactivation.
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