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Nutrition Review Exam 2 > Review Lecture exam 2 > Flashcards

Review Lecture exam 2 Flashcards

1
Q

 Simple Carbohydrates

A

Monosaccharides- single sugars, like glucose, fructose, galactose

Disaccharide- pairs of monosaccharides

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2
Q

 Complex Carbohydrates

A

Polysaccharide- starches and fiber

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3
Q

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

A

only nitrogen is found in protein

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4
Q

 Monosaccharide known as blood sugar

A

Glucose

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5
Q

 Sweetest tasting simple carbohydrate

A

Fructose

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6
Q

 Condensation (disaccharides, triglycerides, and amino acids)

A

Maltose- glucose and glucose

Sucrose- glucose and fructose

Lactose- glucose and galactose

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7
Q

 Composition of the disaccharides

A

pairs of three monosaccharides (fructose, glucose, galactose)

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8
Q

 What glycogen is and where it is stored

A

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

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9
Q

 Enzymes that break down disaccharides (Ex. Maltase)

A

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

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10
Q

Primary site of carbohydrate, fat, and protein digestion

A

small intestine

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11
Q

 Gluconeogenesis

A

Making glucose from a new source (protein)

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12
Q

 How long our glycogen stores can last

A

It’s only stores for less than one day

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13
Q

 Function of insulin, glucagon, and epinephrine

A

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

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14
Q

 Organ of insulin and glucagon production

A

Pancreas

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15
Q

 Features of Type I and Type II Diabetes

A

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

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16
Q

 Normal blood glucose levels

A

70-110

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17
Q

 Hypo and hyperglycemia

A

Hypo is low blood sugar/ glucose

Hyper is high blood sugar/ glucose

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18
Q

 Health effects of regular sugar ingestion

A

Nutrient deficiencies
Empty calories
Dental caries

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19
Q

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

A

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

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20
Q

 % of lipids in foods that are triglycerides

A

Triglycerides – 95% of the lipids in foods.

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21
Q

 Chemical composition of triglycerides

A

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

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22
Q

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

A

Triglycerides

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23
Q

 Kind of fat olive oil is

A

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

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24
Q

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

A

refer to slides

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25
Q

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

A

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

26
Q

 Hydrogenation

A

adding hydrogens back

27
Q

 Cis and trans fatty acids

A

cis is hyrdrogen on the same side of the double bonds

Trans- hydrogen on opposite side of double bonds

28
Q

 Features of cholesterol

A

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

29
Q

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

A

186

30
Q

 Bile

A

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.

31
Q

 Micelles

A

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

32
Q

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

A

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

33
Q

 Chylomicrons

A 
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
34
Q

 Functions of fat

A

energy, protection, insulation, and maintaining cell membrane

35
Q

 HDL and LDL

A

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

36
Q

 Essential fatty acids-Linoleic

A

Linoleic acid (18 carbon) and the omega-6 family

Given Linoleic acid, we can make Arachidonic acid (ARA)
ARA needed for adequate brain development.

37
Q

 Health effects of excessive intake of fats

A

heart disease, diabetes, obesity,

38
Q

 Factor that differentiates one AA from another

A

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

39
Q

 Essential amino acids

A

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

40
Q

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

A

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

41
Q

 Dipeptide, Tripeptide, Polypeptide

A

Dipeptide – two AA bonded together.
Remember condensation.

Tripeptide – three amino acids bonded together.

Polypeptide – many AA bonded together.

42
Q

 Sickle-cell anemia

A

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

43
Q

 Denaturation

A

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.

44
Q

 Primary digestion place for proteins

A

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.

45
Q

 Function of pepsin

A

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

46
Q

 Structure of an enzyme

A

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

47
Q

 Collagen

A

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

48
Q

 Antibodies

A

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

49
Q

 Amino acid pool

A

Amino Acid Pool – remains fairly constant

These amino acids can be used to make new proteins or they can be used for energy.

50
Q

 Protein sparing (in Chapter 4)

A

supply your body witkh adequate carbs to prevent gluconeogenesis

51
Q

 Nitrogen balance

A

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

52
Q

 Protein turnover

A

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

53
Q

 Deamination

A 
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
54
Q

 Quality of a food protein determined by what

A

amino acid composition, and protein digestibility

55
Q

 Marasmus and Kwashiokor characteristics

A

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

56
Q

 Homocysteine

A

amino acid

Homocysteine – independent risk factor for heart disease

57
Q

Nonessential amino acids

A

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

58
Q

Conditionally essential amino acids

A

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.

59
Q

Essential fatty acids- Linolenic

A

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.

60
Q

Essential fatty acids- Eicosanoids

A

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

Fatty acid deficiencies
Rare
Depression

Nutrition Review Exam 2 (4 decks)

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