You have extracted total protein from a mutant virus that lacks any a specific enzyme activity, and discover that the extract contains several very large proteins. You compare this to a similar extract taken from a wild-type population of the same species and discover there are no very large proteins, but you do observe additional smaller peptides. How can you explain this result?
A) Polyproteins are evident in the mutant extract.
B) The mutant lacks the ability to hydrolyse the long proteins.
C) The w/t virus was able to produce protein degrading enzymes.
D) A viral encoded protease was functional in the w/t population but not in the mutant.
E) All the options listed here are correct.

Question

Quizplus · Accepted Answer

All the options listed contribute to explaining the observed results. The presence of very large proteins in the mutant extract suggests that polyproteins are not being cleaved into smaller peptides, indicating a lack of proteolytic activity. This could be due to the mutant virus lacking the ability to hydrolyze long proteins (B), while the wild-type virus produces protein-degrading enzymes (C) and has a functional viral-encoded protease (D) that processes the polyproteins into smaller peptides.

You Have Extracted Total Protein from a Mutant Virus That