By K. Gaede
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A l l the s e q u e n c e w o r k s u g g e s t s t h a t t h e s u b u n i t s a r e i d e n t i c a l 30 M O L E C U L A R BASIS O F B I O L O G I C A L A C T I V I T Y and t h e r e is no c h e m i c a l e v i d e n c e sequences a d d u p to exhausts are about the p o s s i b i l i t i e s 800 a m i n o a c i d s As mentioned and b e i n g 119 a m i n o acids but in e a c h that by no the means because sulfhydryl them enables an i n h i b i t o r These there subunit. before, knowing s h o w s the r a d i o a c t i v i t y they are not.
In this respect the carboxypeptidase-treated enzyme again resembles liver aldolase, which is not inactivated by glyceraldehyde 3phosphate (see Fig. 4 ) , and does not show the enhanced activity towards fructose 1,6-diphosphate. Proposed Mechanism for the Cleavage of Fructose Diphosphate On the basis of this information regarding the nature of the functional groups at the active site of rabbit muscle aldolase we have proposed the tentative mechanism for the dealdolization reaction shown in Fig. 7.
F . 3695 22. 23. (1967). , 3£:245 S m i l l i e , L . B . and M a d s e n , N . B . , J. M o l . B i o l . (1968) . , Biochem. S m i l l i e , L . B . and M a d s e n , N . B . , C a n . M. and Blackman, D . , Biochemistry 25. Battell, M . L . , J. B i o l . C h e m . 243^6202 S h a l t i e l , S . and 39_:1003 28. (1970). S m i l l i e , L . B . and M a d s e n , N . B . , (1968). (1970) . , Biochem. Biophys. Res. , G r a t z e r , W . B . , and V a l e n t i n e , Comm. , (1968) . K e n t , A .