Review Lecture exam 2

Question 1

 Simple Carbohydrates

Answer 1

Monosaccharides- single sugars, like glucose, fructose, galactose

Disaccharide- pairs of monosaccharides

Question 2

 Complex Carbohydrates

Answer 2

Polysaccharide- starches and fiber

Question 3

 Atoms in Carbohydrates, Fats, Proteins (Carbon, Hydrogen, Oxygen, Nitrogen)

Answer 3

only nitrogen is found in protein

Question 4

 Monosaccharide known as blood sugar

Answer 4

Glucose

Question 5

 Sweetest tasting simple carbohydrate

Answer 5

Fructose

Question 6

 Condensation (disaccharides, triglycerides, and amino acids)

Answer 6

Maltose- glucose and glucose

Sucrose- glucose and fructose

Lactose- glucose and galactose

Question 7

 Composition of the disaccharides

Answer 7

pairs of three monosaccharides (fructose, glucose, galactose)

Question 8

 What glycogen is and where it is stored

Answer 8

Storage form of glucose in the body. It’s stored in the liver muscle

Question 9

 Enzymes that break down disaccharides (Ex. Maltase)

Answer 9

Maltase breaks down maltose which is glucose and glucose

Sucrase breaks down sucrose which is glucose and fructose

Lactase breaks down lactose which is glucose and galactose

Question 10

Primary site of carbohydrate, fat, and protein digestion

Answer 10

small intestine

Question 11

 Gluconeogenesis

Answer 11

Making glucose from a new source (protein)

Question 12

 How long our glycogen stores can last

Answer 12

It’s only stores for less than one day

Question 13

 Function of insulin, glucagon, and epinephrine

Answer 13

Insulin- transports glucose from the blood stream into the cells

Glucagon- releases glucose from the liver in response to low blood sugar

Epinephrine- is the fight or flight hormone

Question 14

 Organ of insulin and glucagon production

Answer 14

Pancreas

Question 15

 Features of Type I and Type II Diabetes

Answer 15

Type 1- failure of insulin production and there is no key to unlock cells (cause is unclear) may be genetic, most common in juvenile, but less common than type 2.

Type 2- cells fail to respond to insulin, and are insulin resistant, consequence of obesity.
Complication chd, kidney, disease, amputation, and eye disease. No longer an adult disease

Question 16

 Normal blood glucose levels

Answer 16

70-110

Question 17

 Hypo and hyperglycemia

Answer 17

Hypo is low blood sugar/ glucose

Hyper is high blood sugar/ glucose

Question 18

 Health effects of regular sugar ingestion

Answer 18

Nutrient deficiencies
Empty calories
Dental caries

Question 19

 % of total kcals that should come from carbs, fats, proteins

Answer 19

Carbs 45-65%
Fats- less than 30% of total kcals
Proteins- 10- 35%

Question 20

 % of lipids in foods that are triglycerides

Answer 20

Triglycerides – 95% of the lipids in foods.

Question 21

 Chemical composition of triglycerides

Answer 21

the chief form of fat in the diet and the mahor storage form of fat in the body composed of a molecule of glycerol with three fatty acids attached also called tricylglycerols

Question 22

 Form most dietary lipids are in (Triglycerides, Phospholipids, or Sterols)

Answer 22

Triglycerides

Question 23

 Kind of fat olive oil is

Answer 23

Monounsaturated fatty acids - olive oil, canola oil, peanut oil, nuts, avocados.

Question 24

 What is a saturated fat, mono and polyunsaturated fatty acids - be able to identify structures

Answer 24

refer to slides

Question 25

 Be able to identify the omega number of a fatty acid

Answer 25

Omega number: Omega-3 fatty acid Omega-6 fatty acid

Question 26

 Hydrogenation

Answer 26

adding hydrogens back

Question 27

 Cis and trans fatty acids

Answer 27

cis is hyrdrogen on the same side of the double bonds | Trans- hydrogen on opposite side of double bonds

Question 28

 Features of cholesterol

Answer 28

daily value, roles of cholesterol, endogenous and exogenous, ******************************

Question 29

 Mg of cholesterol in an egg – in a chart on your slides

Answer 29

186

Question 30

 Bile

Answer 30

its an emulsifier that prepares fats and oils for digestion; an exocrine secretes made by the liver, stored in the gallbladder and released when needed.

Question 31

 Micelles

Answer 31

tiny spherical complexes of emulsified fat that arise during digestion, most contain bile salts and the products of lipid digestion including fatty acids, monoglyceride, cholesterol

Question 32

 Fats that are absorbed into the bloodstream vs. those absorbed into the lymphatic system

Answer 32

glycerol and scfa, mcfa, are absorbed in bloodstream, lcfa and monoglycerides in lymphatic system. ************************************

Question 33

 Chylomicrons

Answer 33

``` Chylomicrons Largest and least dense. Mainly triglycerides Cells all over the body remove the triglycerides as chylomicrons pass by. Chylomicron gets smaller and smaller. Remnants in the liver make VLDL ```

Question 34

 Functions of fat

Answer 34

energy, protection, insulation, and maintaining cell membrane

Question 35

 HDL and LDL

Answer 35

LDL = low-density lipoproteins “Lousy” Cells take what they need from LDL Contains few triglycerides, much cholesterol. HDL = high-density lipoproteins “Healthy” Takes cholesterol out of cells to the liver to be recycled or disposed. Scavengers

Question 36

 Essential fatty acids-Linoleic

Answer 36

Linoleic acid (18 carbon) and the omega-6 family Given Linoleic acid, we can make Arachidonic acid (ARA) ARA needed for adequate brain development.

Question 37

 Health effects of excessive intake of fats

Answer 37

heart disease, diabetes, obesity,

Question 38

 Factor that differentiates one AA from another

Answer 38

Carbon atoms must have four bonds so a fourth attachment is necessary, the fourth site distinguish each amino acid from the others.

Question 39

 Essential amino acids

Answer 39

Essential amino acids Must be provided by the diet a.k.a indispensable amino acids 9 essential amino acids

Question 40

 Phenylalanine and tyrosine example (given in class and on your slides)

Answer 40

need essential amino acids Phenylalanine to make tyrosine the body cant convert tryosine also becomes conditionally essential. Phenylketonuria- body can't convert the phenylalanine to tyrosine PKU- avoid phenylalanine, given tyrosine supplements

Question 41

 Dipeptide, Tripeptide, Polypeptide

Answer 41

Dipeptide – two AA bonded together. Remember condensation. Tripeptide – three amino acids bonded together. Polypeptide – many AA bonded together.

Question 42

 Sickle-cell anemia

Answer 42

a hereditary form of anemia characterized by abnormal sickle or crescent shaped red blood cells. Sickled cells interfere with the oxygen transport and blood flow. symptoms are precipitated by dehydration and insufficient oxygen (as may occur at high altitudes) and include hemolytic anemia ( red blood cells burst) fever and severe pain in the joints and abdomen

Question 43

 Denaturation

Answer 43

Protein denaturation Proteins uncoil and lose their shape. Uncoiling of the protein due to heat, acid, agitation. Examples: hardening of an egg when cooked, stiffening of egg whites.

Question 44

 Primary digestion place for proteins

Answer 44

Mouth – crushing and moistening of protein. Stomach HCl Denatures protein Activates pepsinogen (an inactive enzyme) Pepsinogen  pepsin Cleaves proteins – large polypeptides into smaller polypeptides and some AA. Small intestine Proteases Intestinal and pancreatic – further hydrolysis into shorter peptide chains. Peptidases Split dipeptides and tripeptides into single AA.

Question 45

 Function of pepsin

Answer 45

a gastric enzyme that hydrolyzes protein. Pepsin is secreted in an inactive form pepsinogen which is activated by hydrochloric acid in the stomach

Question 46

 Structure of an enzyme

Answer 46

proteins that facilitate chemical reactions without being changed in the process, protein catalyst

Question 47

 Collagen

Answer 47

the structural protein from which connective tissues such as scars tendons ligaments and the foundations of bones and teeth are made

Question 48

 Antibodies

Answer 48

large proteins of the blood and body fluids produced by the immune system in response to the invasion of the body by foreign molecules (usually proteins called antigens) antibodies combine with and inactivate the foreign invaders thus protecting the body

Question 49

 Amino acid pool

Answer 49

Amino Acid Pool – remains fairly constant These amino acids can be used to make new proteins or they can be used for energy.

Question 50

 Protein sparing (in Chapter 4)

Answer 50

supply your body witkh adequate carbs to prevent gluconeogenesis

Question 51

 Nitrogen balance

Answer 51

the amount of nitrogen consumed (N in) as compared with the amount of nitrogen excreted (N out) in a given period of time

Question 52

 Protein turnover

Answer 52

Protein turnover Proteins are being continually made and broken down in the body. The AA made in the liver mix with AA from dietary protein forming your amino acid pool. Amino acid pool – endogenous and exogenous amino acids

Question 53

 Deamination

Answer 53

``` Deamination- removal of the nitrogen group Deamination Stripped of their nitrogen Produces ammonia Liver picks it up, converts to urea Kidneys filter urea out of the blood Nitrogen ends up in the urine. Pg. 227 ```

Question 54

 Quality of a food protein determined by what

Answer 54

amino acid composition, and protein digestibility

Question 55

 Marasmus and Kwashiokor characteristics

Answer 55

Marasmus – severe deprivation of food for a long period of time. (deficient in kcals, protein, vitamins, minerals, etc) Kwashiorkor – protein deficiency Marasmus-kwashiorkor mix Look at slides pg 20,21 on chapter 6

Question 56

 Homocysteine

Answer 56

amino acid | Homocysteine – independent risk factor for heart disease

Question 57

Nonessential amino acids

Answer 57

Nonessential amino acids a.k.a dispensable amino acids The body can synthesize them. 11 nonessential amino acids

Question 58

Conditionally essential amino acids

Answer 58

Conditionally essential amino acids Nonessential AA becomes essential EX: Need Essential AA phenylalanine to make tyrosine (nonessential AA) If diet doesn’t give it or body can’t convert it, tyrosine also becomes conditionally essential. Phenylketonuria – body can’t convert phenylalanine to tyrosine. PKU – avoid phenylalanine, given tyrosine supplements.

Question 59

Essential fatty acids- Linolenic

Answer 59

Linolenic acid and the omega-3 family EPA =eicosapentaenoic acid DHA = docosahexaenoic acid Important in both brain and eye development. Play a role in prevention of heart disease.

Question 60

Essential fatty acids- Eicosanoids

Answer 60

Eicosanoids EPA derived vs. arachidonic acid derived EPA derived eicosanoids help lower bp, prevent blood clot formation, prevents inflammation Fatty acid deficiencies Rare Depression