By J.John Marshall

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N e i t h e r enzyme n e e d s any i o n f o r i t s a c t i v i t y , t h a t i s , t h e r e i s no a b s o l u t e r e q u i r e m e n t ( 2 ) . However, a d d i t i o n of 2+ enhances the a c t i v i t y of both sucrose phosphate s y n t h e ­ Mg t a s e and s u c r o s e s y n t h e t a s e i n t h e d i r e c t i o n o f s u c r o s e s y n ­ 2+ t h e s i s , but M g h a s an i n h i b i t o r y a c t i o n on t h e c l e a v a g e I—> 1 1 1 1 1 1 1 1 A Fraction number FIGURE 1 . Gel f i l t r a t i o n o f w h e a t germ s u c r o s e p h o s p h a t e s y n t h e t a s e p r e p a r a t i o n on S e p h a r o s e 6B.

Thus t h e s e r e s u l t s show t h a t r h a m n o s e , glucose and g a l a c t o s e from l a b e l e d thymidine diphosphate hexoses were i n c o r p o r a t e d i n t o g l y c a n s . In control experi­ ments i t was f o u n d t h a t i n c o r p o r a t i o n d i d n o t o c c u r w i t h 1 4 h e a t e d enzyme e x t r a c t s o r w i t h u r i d i n e d i p h o s p h a t e C-glucose i n place o f the thymidine diphosphate hexoses. I t was c o n ­ cluded t h a t thymidine diphosphate hexoses were t h e p r e c u r s o r s f o r rhamnose, g l u c o s e and g a l a c t o s e o f t h e g l y c a n s .

T h e i r i s o e l e c t r i c p o i n t s a r e o f t h e same o r d e r (see T a b l e I I ) and b o t h enzymes seem t o r e q u i r e s u l f h y d r y l groups f o r t h e i r a c t i v i t y . I n a d d i t i o n to these s i m i l a r i t i e s , both r e a c t i o n s occur v i a equal sequen­ t i a l l y o r d e r e d mechanisms ( 2 0 , 2 1 ) , and s t u d i e s w i t h i n h i b i t o r y s u g a r s - such as ό - g l u c o n o l a c t o n e - s u g g e s t t h a t b o t h r e a c ­ t i o n s take place through the formation of a glucose-enzyme complex i n w h i c h t h e g l u c o s y l u n i t has a h a l f - c h a i r c o n f o r ­ mation.

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