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The change o f t h e c o n t e n t o f t y r o s i n e r e s i d u e i n p e p t i d e Tm shows t h a t o n l y t h e t y r o s i n e a t p o s i t i o n 23 i s m o d i f i e d . ch003 llf R e d u c t i o n o f O z o n i z e d Lysozyme. M e t h i o n i n e s u l f o x i d e can r e v e r t t o methionine w i t h the generation of the l y t i c a c t i v i t y f o r p h o t o - o x i d i z e d l y s o z y m e ( 1 4 ) . We t e s t e d w h e t h e r t h e o z o n i z e d l y s o z y m e c o u l d be r e a c t i v a t e d by c h e m i c a l r e d u c t i o n .

Absorbance spec­ tra were recorded at intervah and changes at 280 and 288 nm were plotted. ch003 3 J 100 I 200 I I I 300 400 0 , , nmoles 2 I 500 600 Figure 5. Separation of ozonized lyso­ zyme CNBr fragments. The ozonized lysozyme was treated with CNBr as described in the Materiah and Meth­ ods. 5 ml/min. Fractions were assayed by measuring UV absorbance on ninhydrin color after alkaline hy­ drolysis. 4 3 ïêmmKuuxaxxxxxy/ 10 20 30 20 40 60 80 EFFLUENT VOLUME (ml) Figure 6. Binding of ozonized lysozyme to CM-chitin.

3 A ) . C o n v e r s e l y , t h e a c t i v i t y o f g l u c o s e 6-phosphate d e h y d r o g e n a s e (G6PD) was u n a f f e c t e d i m m e d i a t e l y f o l l o w i n g t h e o z o n e e x p o s u r e ; b u t w i t h i n 24 h r , t h e a c t i v i t y o f G6PD was s i g n i f i c a n t l y above t h e c o n t r o l l e v e l a n d i t remained t h e r e f o r a t l e a s t 72 h r ( F i g . 3 B ) . A n o t h e r enzyme i n t h e p e n t o s e p h o s p h a t e p a t h way, 6 - p h o s p h o g l u c o n a t e d e h y d r o g e n a s e , showed s i m i l a r t r e n d s t o G6PD ( T i n g e y , u n p u b l i s h e d ) .

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