Flashcards in Review Lecture exam 2 Deck (60)
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Simple Carbohydrates
Monosaccharides- single sugars, like glucose, fructose, galactose
Disaccharide- pairs of monosaccharides
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Complex Carbohydrates
Polysaccharide- starches and fiber
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Atoms in Carbohydrates, Fats, Proteins (Carbon, Hydrogen, Oxygen, Nitrogen)
only nitrogen is found in protein
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Monosaccharide known as blood sugar
Glucose
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Sweetest tasting simple carbohydrate
Fructose
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Condensation (disaccharides, triglycerides, and amino acids)
Maltose- glucose and glucose
Sucrose- glucose and fructose
Lactose- glucose and galactose
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Composition of the disaccharides
pairs of three monosaccharides (fructose, glucose, galactose)
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What glycogen is and where it is stored
Storage form of glucose in the body. It's stored in the liver muscle
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Enzymes that break down disaccharides (Ex. Maltase)
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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Primary site of carbohydrate, fat, and protein digestion
small intestine
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Gluconeogenesis
Making glucose from a new source (protein)
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How long our glycogen stores can last
It's only stores for less than one day
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Function of insulin, glucagon, and epinephrine
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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Organ of insulin and glucagon production
Pancreas
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Features of Type I and Type II Diabetes
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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Normal blood glucose levels
70-110
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Hypo and hyperglycemia
Hypo is low blood sugar/ glucose
Hyper is high blood sugar/ glucose
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Health effects of regular sugar ingestion
Nutrient deficiencies
Empty calories
Dental caries
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% of total kcals that should come from carbs, fats, proteins
Carbs 45-65%
Fats- less than 30% of total kcals
Proteins- 10- 35%
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% of lipids in foods that are triglycerides
Triglycerides – 95% of the lipids in foods.
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Chemical composition of triglycerides
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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Form most dietary lipids are in (Triglycerides, Phospholipids, or Sterols)
Triglycerides
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Kind of fat olive oil is
Monounsaturated fatty acids - olive oil, canola oil, peanut oil, nuts, avocados.
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What is a saturated fat, mono and polyunsaturated fatty acids - be able to identify structures
refer to slides
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Be able to identify the omega number of a fatty acid
Omega number:
Omega-3 fatty acid
Omega-6 fatty acid
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Hydrogenation
adding hydrogens back
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Cis and trans fatty acids
cis is hyrdrogen on the same side of the double bonds
Trans- hydrogen on opposite side of double bonds
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Features of cholesterol
daily value, roles of cholesterol, endogenous and exogenous,
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Mg of cholesterol in an egg – in a chart on your slides
186
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Bile
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.
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Micelles
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
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Fats that are absorbed into the bloodstream vs. those absorbed into the lymphatic system
glycerol and scfa, mcfa, are absorbed in bloodstream, lcfa and monoglycerides in lymphatic system.
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Chylomicrons
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
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Functions of fat
energy, protection, insulation, and maintaining cell membrane
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HDL and LDL
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
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Essential fatty acids-Linoleic
Linoleic acid (18 carbon) and the omega-6 family
Given Linoleic acid, we can make Arachidonic acid (ARA)
ARA needed for adequate brain development.
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Health effects of excessive intake of fats
heart disease, diabetes, obesity,
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Factor that differentiates one AA from another
Carbon atoms must have four bonds so a fourth attachment is necessary, the fourth site distinguish each amino acid from the others.
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Essential amino acids
Essential amino acids
Must be provided by the diet
a.k.a indispensable amino acids
9 essential amino acids
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Phenylalanine and tyrosine example (given in class and on your slides)
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
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Dipeptide, Tripeptide, Polypeptide
Dipeptide – two AA bonded together.
Remember condensation.
Tripeptide – three amino acids bonded together.
Polypeptide – many AA bonded together.
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Sickle-cell anemia
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
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Denaturation
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.
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Primary digestion place for proteins
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.
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Function of pepsin
a gastric enzyme that hydrolyzes protein. Pepsin is secreted in an inactive form pepsinogen which is activated by hydrochloric acid in the stomach
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Structure of an enzyme
proteins that facilitate chemical reactions without being changed in the process, protein catalyst
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Collagen
the structural protein from which connective tissues such as scars tendons ligaments and the foundations of bones and teeth are made
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Antibodies
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
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Amino acid pool
Amino Acid Pool – remains fairly constant
These amino acids can be used to make new proteins or they can be used for energy.
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Protein sparing (in Chapter 4)
supply your body witkh adequate carbs to prevent gluconeogenesis
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Nitrogen balance
the amount of nitrogen consumed (N in) as compared with the amount of nitrogen excreted (N out) in a given period of time
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Protein turnover
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
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Deamination
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
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Quality of a food protein determined by what
amino acid composition, and protein digestibility
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Marasmus and Kwashiokor characteristics
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
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Homocysteine
amino acid
Homocysteine – independent risk factor for heart disease
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Nonessential amino acids
Nonessential amino acids
a.k.a dispensable amino acids
The body can synthesize them.
11 nonessential amino acids
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Conditionally essential amino acids
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.
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Essential fatty acids- Linolenic
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.
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