The Self-Digesting Problem of Analysing Properties of Pancreatic Serine Proteases
A major difficulty in investigating the properties of pancreatic serine proteases is that these enzymes, being proteins, are self digesting. The problem is less severe for solutions of chymotrypsinthan than for solutions of elastase or trypsin.
Suggest an explantion for this observation?
(Do not consider the zymogen activation steps (Chymotripsinogen to chymotrypsin) but only the final active form of these proteins.)
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Chymotrypsin cleaves the peptide bond on the carboxy-terminal side of large hydrophobic residues like phenylalanine, tyrosine and tryptophan. These residues, because they are nonpolar, are likely to be buried in the interior of globular proteins. As a result, they are generally inaccessible to ...
Solution Summary
The solution gives a clear, descriptive explanation for the discrepancies in self-digesting abilities of solutions of chymotrypsinthanin than elastase or trypsin in terms of their differences in cleavage sites.