364 Prof. H. E. Armstrong and Dr. E. F. Armstrong. [May 9, 



a-glucoside. But independent proof of its character is afforded by the fact 

 that the primary product of the hydrolysis of maltose is a-glucose (1.1307). 

 Maltose and apparently lactose also appear to differ from cane sugar in that 

 they are hydrolysed by enzymes which also act on the corresponding simple 

 glucosides (monosides). 



The existence of this difference affords further proof that the configuration 

 of cane sugar and of its correlative enzyme are peculiar and altogether 

 different from that of other bioses and biases. To account for the wider 

 activity of a biase such as maltase, it is only necessary to suppose that not only 

 are the simple glucosides of the same general type as the correlative bioses, 

 but that this resemblance also extends to the biases and that it is sufficient 

 in some cases if the attachment of the biase be secured over one section of 

 the hydrolyte. Thus, representing the glucose radicle by G and other radicles 

 such as are present in simple glucosides by E, E^ being the hypothetical radicle 

 of the enzyme correlative with the radicle G, the following diagram may be 

 used, the horizontal line representing the section of the molecule over which 

 attachment of enzyme to hydrolyte takes place — 



G. O.G 

 W . E^ 



G. .E 



E? . E? 



Formation of Enzymes. — It is conceivable that the enzymes themselves are 

 subject to hydrolysis and simplification — in other words that a biase may give 

 rise to a monase. The existence of monases in admixture with biases is, 

 therefore, to be expected. Attention has already been called in the previous 

 communication to evidence indicative of the presence in extracts of dried 

 yeast of an enzyme (a-glucase) capable of hydrolysing methyl- a -giucoside, but 

 without action on maltose ; this discovery may well prove to be significant 

 from the point of view now advanced. 



There can be little doubt that the sucroclastic enzymes are products of 

 hydrolytic changes conditioned by enzymes (mainly by proteoclasts, in all 

 probability) ; the very different results obtained with extracts prepared under 

 different conditions (at different temperatures, etc.) are scarcely to be 

 accounted for in any other manner. And it is to be supposed that several 

 enzymes may arise in this manner, all of one type, yet all capable of 

 hydrolysing a particular hydrolyte and differing only in activity, much in the 

 same way that the various simple glucosides represented by the general 

 formula E'.O.G. (such as methyl-, ethyl-, phenyl-glucoside, salicin, etc.) differ 

 in stability towards hydrolytic agents. 



