6. Would you expect elasmobranchs to have high concentrations of the enzyme urea
ID: 261743 • Letter: 6
Question
6. Would you expect elasmobranchs to have high concentrations of the enzyme urease in tissues? Explain. 7. Design an experiment to determine, within 0.1 pH units, the pH optima of the enzyme pepsin. 8. How does pepsin digest proteins? 9. Would you expect pepsin to be active in the anterior small intestine? 10. What is the purpose of incubating the film strips with water? Is in the alpha amylase experiment? Would they have to be done everytime the experiment was performed? 12. In the alpha amylase expe sugar test in the same assay? nment, is it possible to get a negative starch and a negative reducing 13. Why was it necessary experiment? Why wasn't it done in all of the experiments? to equilibrate the solutions to the proper temperature in the alpha amylase 14. Do you think the alpha amylase experiment was properly controlled? What other controls could or should have been done? 15. Which test is the more sensitive assay for alpha amylase activity, the IKI test or the reducing sugar test? Explain why you chose your answer. 16. Is it possible for an enzyme to be unaffected by increasing temperature while still observing a decrease in rate of reaction with increasing temperature? Describe some conditions under which this might occur
Explanation / Answer
6) No, elasamobranchs doesnt have high concentration of urease in tissue because urease hydrolyze urea into carbondioxide and ammonia . Elasmobranchs ( sharks, ray) retain urea in tissue and body fluid at concentration as high as 0.6M as a mechanism of osmoregulation in salt water environment. So, to maintain high concentration of urea , urease is not present in high concentration. Recent finding indicates that existance of urease +ve bacteria is compelling because of microbiological species of bacteria inhabiting healthy elasmobronchs tissue. For elasmobronchs host, these endogenous bacteria could confer the requisite urease activity that elasmobronchs require but do not inherently posses.
8) The acid in the stomach causes food protein to unfold in a process called denaturation. It exposes the protein' s bonds so that pepsin can access them and break the protein into smaller fragments called peptide or polypeptide.
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