What is the role of pepsin and pancreatin in protein digestion? Where can these enzymes be found in the body? Role of pepsin Pepsin is found in : Role of Pancreatin Pancreatin is found in :
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SPECIFY THE FUNCTIONS FOR EACH ENZYME PRESENT FOR PROTEIN DIGESTION
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- 7. To improve the digestion of food proteins in chronic inflammatory-dystrophic disorders of the pancreatic gland, stomach or intestine patients are prescribed mezym forte (pancreatin) containing pancreatic enzymes. What is the remedial mechanism of this drug? For the answer: a) enumerate enzymes digesting proteins in the gastrointestinal tract; b) specify the mechanism of proteolytic enzyme activation; c) draw the schemes of these enzymes activation, point out the activators; d) explain the specificity of proteases; e) describe the consequences of these enzymes activation in the tissue of pancreas.Match the water soluble vitamin with its main function. coenzyme specifically with tryptophan metabolism, hemoglobin Choose... DNA, RNA, cell division Choose... thiamin, riboflavin, niacin vitamin C antioxidant, collagen synthesis, redox B12 Folate coenzyme B6 Choose... DNA, RNA, methionine metabolism >6. Why would the lack of lactase cause Carol so much distress? Where would the undigested lactose travel from the small intestine. a) what could the production of gas from the breakdown of sugar. 7) Are enzymes only important for digestion, as is the case with lactase? 8. Why would it be important to regulate the function of an enzyme at all? Please read the reading, and then answer the questions.
- 2. The patient's blood glucose concentration was 160 mg/dL 30 minutes after taking 100 g of sugar. The blood glucose level of the same patient 30 minutes after cating 100 grams of bread was lower. Why? To answer: a) draw the structures of sucrose and starch; b) describe the digestion of these carbohydrates, indicate the enzymes, the site of their synthesis, and the parts of the gastrointestinal tract in which the hydrolyzis of sucrose and starch occurs.4. Lactose Intolerance (Enzymes) Carol was recovering from a terrible bout with the flu, having been sick for nearly two weeks. As she was getting her strength back, her appetite also improved. In fact, after not eating very much for almost two weeks, Carol was famished. But something strange happened to her: When she began eating milk products after the illness, she experienced terrible abdominal distress-she had bloating, pain, and diarrhea. Carol went to see her doctor and explained her symptoms. Her doctor said that the virus she contracted must have affected the enzyme-producing cells in her small intes- tine. Carol had become lactose intolerant. Whenever she ate any food containing milk, her digestive system was unable to break down the sugar in the food or beverage. Her doctor suggested that Carol stay away from dairy products, except for yogurt. Last night Carol saw you studying your biology textbook in the library, and she asked you to explain some things to her.6. More enzyme activity.... A) Discuss how proteolytic cleavage is used to achieve tight control of the activity of digestive enzymes. B) If proteolytic cleavage leads to irreversible activation of digestive enzymes, how is the activity of digestive enzymes reduced when no longer needed? There were two ways presented this semester. C) We looked at three serine protease enzymes: elastase, chymotrypsin, and trypsin. All three enzymes cut peptide bonds using a similar catalytic mechanism. Explain why these are called serine proteases. D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
- 3. A patient has got excess carbohydrate meal for the years and gain the weight. To explain this: a) draw the schemes of TAG synthesis in the liver; b) describe the transport of TAG from the liver to adipose tissue; c) describe the functions of insulin in the conversion of glucose to TAG in the liver and adipose tissue. Glucose containing Catoms was added to isolated hepatocytes inanexperiment. Ifthe glucose was added in excess, the rate of triacylglyccrol synthesis increased.3) Consider the structures of the siderophores ferricrocin (left) and enterobactin (right) below. OH HO, ÓH NH Он HO OH HN. но. HO но1. Is the reagent used to cut peptide bonds during amino acid analysis. 2. Is the name of the amino acid present in the active site of carbonic anhydrase. 3. Is the name of the reagent used to poison serine proteases. Is a component of bacterial cell wall other than N-acetylglucosamine? 4. 5. Is the optimal pH of lysozyme.
- Choose the correct prosthetic group of the given protein. 1. Carbonic Anhydrase 2. Zinc 3. Glutathione 4. Ovomucoid 5. Albumin 6. Mucin 7. HDL 8. Ceruloplasmin 9. Cytochrome 10. Insulin 11. Enkephalin 12. Chromatin 13. Vitelline 14. Collagen 15. Casein 16. ADH2.A person did not get food for 3 days and had lost his weight, ketone bodies were revealed in urine. To explain this: a)describe the main metabolic pathways providing energy for the liver cells during starvation and explain its regulation; b) discuss the hormonal changes; c)predict the deleterious effect of prolonged starvation.(a) What is the charge of bile acids in the small intestine, where the pH is 7–8? (b) According to one hypothesis, bile acids are toxic to bacteria and so could help limit their growth in the intestine. Propose a mechanism for this bactericidal activity.