1. A patient with poorly controlled Type I diabetes has blood drawn and finds that the pH of his blood is 7.1. The normal pH of blood is 7.4. The patient’s blood [H+] is A) one fourth normal B) one third normal C) half normal D) twice normal E) three times normal 2. The Henderson-Hasselbalch equation: A) allows the graphic determination of the molecular weight of a weak acid from its pH alone. B) does not explain the behavior of di- or tri-basic weak acids C) employs
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environment‚ meaning the semiliquid becomes alkaline. This is when the intestinal digestion begins. The pancreas secrets pancreatic fluid into the intestine. This fluid contains‚ Amylase‚ Trypsin‚ and Lipase. Amylase is released first in the fluid. Amylase breaks down starches into their component sugars. Trypsin hydrolyzes polypeptides‚ converting them into amino acids. Lipase breaks down fats into glycerol and fatty acids. The bile acids produced by the liver act as natural detergents to dissolve
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activation energy of a reaction. All biochemical reactions are catalyzed by enzymes. Since enzymes are proteins‚ they can be denatured in a variety of ways‚ so they are most active under mild conditions. Most enzymes have optimum activity at a neutral pH and at body temperature. Enzymes are also very specific – they only act on one substrate or one class of related substrate molecules. The reason for this is that the active site of the enzyme is complementary to the shape and polarity of the substrate
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HUN 4446 Exam 2 Study Guide Lactose Mal Digestion/ Malabsorption 1. What are the products of lactose digestion? -The products of lactose digestion are glucose and galactose. 2. What is lactase deficiency? -Lactase deficiency is a deficiency in the enzyme that breaks down lactose. The causes of lactase deficiency include congenital defects‚ secondary lactase deficiency‚ and primary (acquired). 3. Define lactose maldigestion‚ identify the potential etiologies of lactose maldigestion‚ and describe
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Observe any digestion of egg white – 5.0 ml water + few grains of bile salts • Tube 2 – 5.0 ml pancreatin • Tube 3 undigested – 5.0 ml pancreatin + few grains of bile salts digested Experiment #3: Fat Digestion • Test pH of each solution w/ pH probe – rinse probe w/ detergent after each test • Place in 37°C bath •
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Enzymes An enzyme is a protein used to speed up the rate of a chemical reaction. Because they regulate the rate of chemical reactions‚ they are also called catalysts. There are many‚ many different types of enzymes‚ because for each chemical reaction that occurs‚ an enzyme specific to that reaction must be made. To act on a substrate‚ an enzyme must contain an active site. The active site is the area on the enzyme that allows the substrate and enzyme to fit together. The amino acids that are present
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microbes before exposed to gastric juices Mouth Tongue Used more by cattle and goats (also use lips) Teeth No upper incisors Used more by sheep (use lips to “sort” feed) Saliva Continual production Cattle: 12 gal/d vs Sheep: 2 gal/d No enzymes; High pH Esophagus No sphincter valve Opens into reticulum and rumen Muscle contractions move in both directions Stomach compartments Reticulum Rumen Omasum Abomasum A higher proportion of a ruminant’s digestive system is stomach Reticulum characteristics
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purpose of this experiment in a way that conveys information to the reader about Amylase’s ability to withstand acidic or basic pH. To do this‚ two test tubes were both filled with 5mL of a 5% amylase solution. The first one was filled with an acid‚ while the other was filled with a base. After dropping liquid Iodine and Benedict’s solution into each one‚ the tube with a basic pH tested positive for glucose. The acidic solution tested (mostly) negative for glucose‚ although there were trace amounts at
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enzyme concentration on the rate of reaction‚ in this case the breakdown of protein by protease enzymes. Aim – Milk powder contains a white protein called casein. A white suspension of milk powder clears on the addition of the enzyme trypsin. The aim of this experiment is to investigate the effect of enzyme concentration on enzyme activity. We will observe how fast the milk turns transparent by changing the concentration of
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on the substrate with particular enzyme functional groups are initiated inducing a conformentional change from a low catalytic enzyme to a high catalytic enzyme (Silverman 2002). The rate of enzyme controlled reactions is dependent on temperature‚ pH‚ and concentration of the substrate and enzyme. If the concentration of a substrate is increased‚ the rate at which product is formed also increases‚ up to a maximum value (The Cell). The kinetic parameter frequently used to characterise an enzyme
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