n km 



reaction is, however, tin- Bame ;it whatever rate il 



enzyme does nol appear in the final product* M 



diastase can be found unaltered in amounl 



their action. This is determined bj adding a 



(thai is, of material tn be acted <»n . when the 



;i'_ r ;iin in the usual way. The Bame is no doubl tru< 



though as yel it can actually be proved for only I. 



therefore, may I"- defined as catalysts produced by li 



The Properties of Enzymes 



Although enzymes are exampli i 'litiit mai 



ties thai appear t<» differ i"i< >in those of inorganic c 11 ill. 



therefore, 1"' advisable in considering m quality I in 



catalysts ami enzymes, for by ibis method a much clei 

 tlic nature of enzyme action can 1'-' gained Bayliss l 



that are Btrictly peculiar t<i enzyn ■ shall 



1. Most enzymes an remarkably specific in tl 

 ganic catalysts <n-< very much /■ Thus, in th< 



which bring about inversion of disaccharides, this sp< sific irly 



shown. There is a s| ial enzyme for each "t" tin- three >\ 



maltose, lactose ami cane siiL r ar and one i 

 another. 



Still more Btrikingly is this specificil inzyme 



in the fad that certain enzymes, Buch as zymasi 

 will act only on bodies having a certain configuration, tl 

 their Bide chains arranged in a certain wa} Tl 

 of dextrose ■< and 8 which differ from each 

 • that the Bide chains are arranged in differenl i 

 tion f«> the centra] chain of carbon atoms This form a is 



called stereoisomerism because the two bodi< 

 i lighl t" an equal degree in opposite din 

 of these hut ool on the other, ami th« r innum< 



same kin. I. [ndeed, of all bodies that ■ nl\ 



one is found in living cells and it is on this variety 



in animals .-an act. A similar specificil 



their pharmacological action. 

 Specificity <>t" action is explained bj - 

 d the Bubstrate ami th. 

 place the enzyme must p 

 rately w ith that of the subsl 



h.ck ami ke\ ; the key mu 



operate. The .p. eificitj d i 



