Abstract
Dry irradiated lysozyme (mucopeptide N- acetylmuramylhydrolase , EC 3.2.1.17) and its fractions have been subjected to kinetic studies. The aggregation of heavily damaged products is delayed by substrates, indicating a possible involvement of the active site in the aggregation process. The activation energy, E a,app , for γ-irradiated lysozyme, and the apparent affinity constant ( K a,app for irradiated lysozyme and its salt-soluble fraction, F-II, are the same as the observed with native enzyme. However, the maximum velocity ( V) decreases with irradiation. Heavily damaged fraction, F-I, or salt-insoluble products are almost inactive. Difference spectra of losyzyme-glycol chitin complex show simlar characteristics for native, irradiated lysozyme and its F-II fraction. However, F-I fraction spectra present abnormal characteristics, indicating alterations in or around a tryptophan moiety. It is proposed that unstable damaged enzyme molecules suffer further modifications during fractionation resulting in enzyme inactivation.
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