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- Determine the location within the human body where each of the following aspects of carbohydrate digestion occurs. 1. The enzyme sucrase is active 2. Hydrolysis reactions converting polysaccharides to disaccharides occur 3. First site where breaking of glycosidic linkages occurs 4. The monosaccharide glucose, fructose, and galactose are produced 5. Pancreatic enzyme is active 6. Hydrolysis reaction converting disaccharide to monosaccharide occur 7. Monosaccharide enter the bloodstream 8. The primary site for CHO digestion is located here. 9. Gastric juice is present 10. Salivary amylase is present here.1. With the prevalence in food of peeled cereals or bread made from high-grade flour, hypovitaminosis B1 may occur. Explain the role that vitamin B, plays in the body. For this: a) name the coenzyme which contains vitamin B, and enzymes, which require this cocnzyme to function; b) write the process in which these enzymes are involved and explain how the process speed will change with a lack of B,; d) what discase develops in the absence of vitamin B,.1. TRUE OR FALSE a) Higher Rf value will be obtained from dextrin than that of glucose in a reverse-phase TLC. b) Salivary amylase is used to hydrolyzed α(1à4) glycosidic bonds in carbohydrates.
- Arrange the following statements regarding the processes of protein metabolism starting from Step 1 to Step 10. Conversion of pepsinogen to pepsin by HCI • Active transport takes place • Conversion to individual amino acids Glutamate becomes alpha-ketoglutarate Mechanical digestion to go to the small intestines • Shuffling of amino group to generate glutamate • Conversion of proteins to simpler polypeptides Removal of basic and acidic functional groups Enters the Kreb Cycle • Acidic denaturation and hydrolysis of proteins3. 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.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.
- (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.Select the enzymes that play a role in producing monosaccharides absorbed by SGLT1. Group of answer choices Pancreatic alpha-amylase Sucrase Maltase Isomaltase Lactase alpha-amylase beta-amylase Glucoamylase Pullulanase Endoglucanase Exoglucanase Cellobiase All of the above1. What is the optimum pH and temperature for salivary amylase?
- 21. The product CREON (pancrelipase) contains 3000 units of lipase, 9500 units of protease, and 15,000 units of amylase in delayed-release capsules. The capsules are to be swallowed whole or the contents added uncrushed to food immediately prior to administration. The dose should not exceed 2500 lipase units/kg of body weight. If a child weighing 24 pounds ingests five CREON capsules, has he exceeded the maximum dose?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?Arrange the following statements regarding the processes of protein metabolism starting from Step 1 to Step 10 Acidic denaturation and hydrolysis of proteins Enters the Kreb Cycle Mechanical digestion to go to the small intestines Shuffling of amino group to generate glutamate Active transport takes place Removal of basic and acidic functional groups Conversion to individual amino acids Glutamate becomes alpha-ketoglutarate Conversion of pepsinogen to pepsin by HCl Conversion of proteins to simpler polypeptides