Enzymology in the Practice of Laboratory Medicine. by P. Blume, E.F. Freier

By P. Blume, E.F. Freier

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Sample text

The slope, compensation t e m p e r a t u r e , cannot be determined with high accuracy with the data available. Howe v e r , the slope is considerably high than found with f e r r i hemoglobin, ligand-binding reactions and with s e v e r a l other proteins. It is also higher than found in any of the other r e actions of chymotrpsin. The main importance of the figure aside from its demonstrations of the compensation pattern i s to show that the slope need not be n e a r 290°K which value h a s previously been used to implicate liquid water a s a direct r e actant.

The n m r r e s u l t s c a r r i e d out under conditions of low dimer concentration may be more reliable than the crystal x - r a y diffraction data but also involve some interpretation which may prove i n c o r r e c t . **According to J . Richards and coworkers (to 37 RUFUS LUMRY we accept it, does little to provide any special electronic m e c h anism for catalysis since a group with such low basicity cannot help an imidazole group extract protons from a substrate or from the SEE 195 hydroxyl group.

If water is held in the s i t e , according to this picture it cannot be bound well since the free energy of its displacement would easily exceed 8 k c a l / m o l e . There is considerable argument a s to the number of water m o l e cules in the s i t e . The data of Blow and c o w o r k e r s 7 7 > 7 8 and of Tulinsky and Vandlen^8 a r e in poor agreement on this m a t t e r a s on numberous other fine details of the positions and mutual r e l a tionships of the functional groups thought to be involved directly in bond r e a r r a n g e m e n t .

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