The specificity of trypsin is determined by on the enzyme. The specificity of elastase is determined by on the enzyme. Three amino acids: Asp, His and Ser, of form a triad to cleave peptide bonds of a substrate.

Another Asp in something like a deep pocket; a superficial amino acid binding pocket with either a slight neutral side, neither elastase nor trypsin.  

Explanation:

Almost all trypsin as well as elastase contain catalytic triads. In trypsin, aspartate is the essential amino acid throughout the bag. The latter's pocket also becomes unique to charged particles (+) side-chain creatures.  Elastase seems to have a pocket which really combines multiple valine residues, making it extremely difficult to reach the pocket with large bulky main chain, this therefore prefers short side chains.

The homologs with chymotrypsin include trypsin but mostly elastase. As either a central amino acid, chymotrypsin encompasses serine.

Sapling B

Explanation:

Since month 2 is the first month that is a point that has an ordered pair, you would take 10/2, which is, and Sapling A has its first full ordered pair at 50,3 then you would take 10/3, which is 3.3. So 5 is greater than 3.