Sandbox 50: Difference between revisions
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In order for trypsinogen to be converted to trypsin, a pro-peptide must be cleaved from trypsinogen. The image at the left shows which sequence is removed from trypsinogen, and the active site of trypsin becomes accessible for its protein substrate. | In order for trypsinogen to be converted to trypsin, a pro-peptide must be cleaved from trypsinogen. The image at the left shows which sequence is removed from trypsinogen, and the active site of trypsin becomes accessible for its protein substrate. | ||
[[Image:Trypsinogen.gif |thumb]] | [[Image:Trypsinogen.gif |thumb]] | ||
==Inhibitiion and Activation== | |||
===Trypsin Inhibition=== | |||
Trypsin inhibitors are generally known as serine protease inhibitors or serpins. Serpins act as competitive inhibitors so they bind to the trypsin active site, rendering the enzyme inactive. There are four natural sources of trypsin inhibitors -- bovine pancreas, ovomucoid, soybeans, and lima beans. Each of these natural sources of inhibition work in different ways. Inhibitors from soybeans and lima beans inactivate insect proteases, acting as a feeding deterrent. Inhibitors from soybeans have also been found to cause pancreatic hypertrophy in rats, also acting as a feeding deterrent in this case. Other trypsin inhibitors include Ag+, benzamidine, ethylenediaminetetraacetic acid EDTA, and diisopropylfluorophosphate (DFP). | |||