final minus lipids, carbohydrates,minerls.txt

chemically unrelated organic substances that are grouped together because each is essential in the diet in minute amounts and is required for specific metabolic reactions.

macronutrients

synthesis of acetylcholine (neurotransmitter) and lecithin (phospholipid).

you can make it in your body but not going to make enough.

• coenzyme in metabolism
• do not produce any energy important for energy production.

• part of the coenzyme Thiamin pyrophosphate. (involved in energy metabolism)
• on membranes of nerve cells. (relies on thiamin for function)

• Beriberi
• damage to nervous system, heart, & other muscles.
• Seen when white rice is a staple food.

in alcoholics 4:5 are deficiant in thiamin b/c causes discreation of thiamin.

• decrease water soluble vitamins
• this case heat actually destroys it.

energy metabolism

multiple

inflammation of mouth, skin, and eyelids; sensitivity to light.

not going to see a lot of.

part of coenzymes nicotinamide adenine dinucleotide (involved w/ energy metabolism) and NADP

• 1. Diarria
• 2. Dermatits
• 3. demantia
• 4. death

when corn was staple food would see this happening.

• not going to see unless supplimenting.
• capillaries will dialate and cause a tingle sensation that can be painful.

• part of coenzyme used in energy metabolism, fat synthesis, amino acid metabolism, and glycogen synthesis.
• involved with TCA cycle
• going towards storeage and breaking down.

• Binds biotin
• -in raw eggs
• rare to see

• involved in fatty acid bio-synthises and also F.A. degradation
• component of coenzyme A
• 70 different enzymes need this coenzyme (CoA or ACP)

• part of coenzyme PLP and PMP?
• -amino acid metabolism
• -serotonin synthesis
• -Heme synthesis

PLP involved w/ making serotonin from tryptoptian involved w/ appetie

• sleep regulation
• neuro transmitter
• sinsory perception (mood)

• Depression and confusion
• -neurotransmitter not made
• microcytic anemia
• -can't make hemengloben
• unable to carry sufficiante amount of o2 to blood.

• fatigue
• headaches
• nerves damage
• can get to this level
• associated w/ neurological damage

• Part of coenzyme THF
• the movement of single C's important for DNA synthesis
• purine synthesis
• also involved w/ B12

• folate supplementation decreases spinal bifida
• started fortifying grains in 1996
• fortification has worked and decreased birth defects.

• imcumplet closing at spinal cord -paralysis, club feet, dislocated hip, curvurture of spin.
• happens durring pregnancy

• higher homocysteine levels in blood increase cardio vascular disease
• damage vascular cells

increase homocysteine

megaloblastic Anemia

• you dont synthasise DNA properly in red blood cells
• RBC's get large but dont divide
• keep swelling and cant make new ones

Oxygen

• absorbed in small intestin
• most deficiencies due to this system not working right
• can occur in older age

• Folate metabolism
• normal function as nerve cells

Convert folate coenzymes to active forms.

maintain the myelin sheath that insalates nerve fibers from each other for proper function.

patchy destraction of myelin sheath

can lead to creeping paralysis or death

pernicious anemia

• 1st sign megablastic anemia (folate deficint)
• -weakness, sore tongue, back pain, and tingling in extremetie

• left untreated can lead to permanent damaged nerve strengths, creeping paralysis
• 10-20% of older adults get this

supplementation of folate improves anemia but still get nerve damage

• Animal products
• vegetarians need to supplement this

• Collagen synthesis
• antioxidant
• iron absorption
• reacts with other food components
• decreased risk of common cold

• Connective tissue
• bone
• teeth
• tendons
• blood vessels
• increases the cross-connection between amino acids making collagen stronger.

• electrons to free radicals which avoids oxidative stress.
• helps vit. E stay in active form

• iron in its most absorbable form
• increase vit. C can = too much iron absorption and toxicity

• 1.reactivates vit. E so that it can be reused
• 2. decreased formation of nitrosamines for nitrite
• -may decrease some cancer

• activity of certain immune cells
• doesn't decrease cold, but may shorten the time you have it.

• Scurvy
• take 20-40 days to become deficient

• Weakness
• open wonds
• bleeding gums
• bleedning around hair follicles

• Nausea
• abdominal cramps
• diarrhea

Heat

ATP and Creatine

ATP and Creatine

• decrease in ph
• causes muscle pain/burning
• fatigue

Muscle releases Lactic Acid into liver then filters it, converts it to glucose.

• Strength and agilitys
• split seconds of power

ex: tennis serve, lefting weights, burst of speed

• endurance,
• low and moderate entensity over a long duration
• dependent more on fat

ex: long swim, hiking, jogging

• 1. what is available from the diet
• 2. the intensity and duration of avtivity
• 3. degree in which body is conditioned to perform.

will last during exercise which influences performance.

influence endurance

better performance

• - glycogen
• - fat

Faster

Not only diet but the activity

physical exertion becomes nearly impossible.

after a few hours of strenuous activity (aerobic) glycogen gets depleted.

happens to marathon runners

• - During last stages of endurance activity glucose consumed during the event goes from G1 to muscles providing needed glucose.
• - eating w/in 15 min. accelerates glycogen. high glycemic foods are better

• get glycogen stores as high as possible
• eat little carbs

• do not want to do this often can cause anhythmias
• maybe do it 2-4 times a year

it provides a lot of energy.

over 20 minutes

higher less fat will be used

allows body to adapt. and use more fat. you get more mitocondria out of this.

Substances or devices that enhance energy production, use or recovery and provide athletes with a competitive advantage.

includes all the reactions by which the body obtains and spends the energy from food.

- Sum of all chemical reactions that take place in living cells.

• -Energy you get from eating plants/animals.
• -Dont get all the energy.

Glucose

-Main use

Glycerol + Fatty Acids

-Main use

Amino Acids

• -primarily for building protein
• - 10-15% comes from protien

Smaller molecules are put together to build larger molecules.

-Have to put energy in to occur

in metabolic pathways dependent on the metabolic state of the person.

fed vs. fasted

Large molecules are broken down to small molecules

-energy is released

• glycogen
• fat (main way)

ATP

Common high energy storage compound.

-As we start to release energy it is temporarly stored in ATP.

- During chemical reactions

ATP and parent compound

Used to transfer energy released during catabolic rxn's to power its anabolic reactions.

• -Heat is released when happening about 60% is heat.
• -some energy is lost as heat

3

2

complex organic molecules that work with enzymes to affilate activity.

Glucose

Were they enter metabolisum.

Glucose

Glucose

ACetyl CoA which is why they can not form glucose

Glucose

the electron transport chain and are used to make ATP

glycolysis

energy

Oxygen has to be present, if not goes towards lactate

Does not have oxygen?

oxygen availability

lactic acid

glucose

2 carbon compounds combined with COA to form Acetyl COA

called fatty acid oxidation

3 carbon compound

used to go towards glucose

• 1. glycerol (3 carbon comp.) enters as pyrubate
• 2. The assetal CoA fatty acid entering the TCA cycle
• 3. NADH and FADH2 from fatty acid that enters the electron train.

can enter as intermediates of the TCA cycle

glucose

this will be important when we consider a long term fast.

• 1. betahydrocsbutarate
• 2. Acetoacitate
• 3. Acetone

Produces small amounts

always have some in system

Reduces loss of appitite

your brain gives up telling you that you are hungry.

low carb diets can force you into this

The specific gene sequence differences between humans and how these affect the differences in repsonses to diet and particular needs for nutrients.

• The study of the effects of diet on the expression of all genes and their functions
• What are the 2 major classifications?
• Fat Soluble and Water Soluble

Vitamin A

• Retinol
• retinal
• retinoic acid

• found in plants
• you get it from eating carrots

• maintains the cornea
• transparent membrane caring the outside of the eye

Rhodepsin

made up of protein opsin and 1 molecule of retinal.

Cells that line any surface that has contact with outside

Vitamin A.

Vitamin A deficiency

1st level; when retinal does not receive enough retinal to rejuvenate visual pigment.

• full blindness
• no vitamin A at cornia.
• Will get hard and dry which is (reversable)
• Then eventually very soft (irreversable)= blindness

• skin cells start making keratin
• gets dry, rough, and scaley

Biological activity is to act as a antioxidant that can deactivate free radicals.

• infectious disease
• night blindness
• blindness (xerophthalmia)
• keratinization

• Bone defects
• Birth defects
• Acne treatments
• Excess beta- carotene leads to skin discoloration

Excessive vitamin A can weaken bones and cause bones to be more prone to fractures

Consumes high amounts. About 7th week of pregnancy can happen.

Acutane-causes birthdefects-> vitamin A

• 1. enhance absorbtion and the GI track
• 2. increases reabsorbtion in kidneys
• 3. increases mobilization from bones to blood.

• Rickets
• osteomalacia
• can occur in older adults

• In children- causes growth retardation, happens when bones fail to calcify
• bones weak and bend (boned legs)

Adults form of rickets

• in women with repeated pregnancy
• low sun exposer
• low calcium intake

• 1. skin, liver, kidney less cappable of making vitamin D
• 2. don't drink much milk
• 3. Don't go outside

• high vitamin D intake causes:
• calcium stones in soft tissue such as kidneys

alpha in humans

Bursting of red blood cells occurs when poly unsatturated fatty acids in cell membrain of red blood cells oxidize RBC's break open and spill contents

can occur in infants

Bacteria and GI track

Vitamin K so not defestiont

• synthesis of bone proteins
• blood clotting
• if you don't have vitamin K proteins cant bind calcium.

excesive bleeding because not forming blood clots.

• bacteria synthesis
• liver
• leafy green vegetables
• Energy Balance is?
• amount of fat stored or used in a day is dependent on energy balance.
• 1lb. fat = 3500 calories
• excess energy is stored as fat
• we eat to refill our body

• Tries to control how much energy comes in by affecting food intake.
• controls when to stop/start eating

amount of heat released when you burn the food.

measure the amount of oxygen consumed

energy out

achieve energy balance

children are good at this

physilogical need for food

• response to seeing or smelling food.
• full (not hungry) but still eat pie

signal to stop eating

signal of don't start eating again.

supresses hunger and inhibits eating the most

• causes carbohydrate cravings
• decreases energy used
• initiates eating.
• increases fat storage

• secreted by stomach cells
• stimulates appitite,
• promotes energy storage

• suppreses appitite,
• increases energy expetiager

easy measurement of how your body uses energy.

only very few people dont produce enough leptin

average person produces enough and given leptin does nothing for them.

the amount of energy expended.

• macronutrients used to make ATP
• rest is lost as heat.

ATP and the rest lost as heat.

the rate of energy used for metabolism under specified conditions

this is what we refer too when talking about ppl havinga fast or slow meabolism.

energy needed to maintain life when a body is at complete digestive, physical, and emotional rest.

• less restrictions then BMR
• criteria for recent food intake and physical activity

voluntary movement of skeletal muscles and support systems.

most variable and most changeable component of energy expenditure.

• 1. muscle mass
• 2. body weight
• 3. activety it's self

• an estimation of the energy required to process food.
• to digest, absorb, transport, metabolise, and store ingested nutrients
• approximately 10% of energy intake

Adjustments in energy expenditure related to changes in environment and to physiological events.

bodies ability to adjust to the situation

proportions of muscle, bone, fat, and other tissue that make up a persons total body weight.

Difficult to measure body composition in living humans so we use body weight.

bone, muscle, water

• body fat
• a sedentary person can be at a healthy weight, but have too much fat.

fat deposited around organs

upper body fat mainly associated with heart disease, stroke, diabetes, hypertension, and some cancers.

• by good health
• BMI is commonly used for this.

weight/height

process by which food is broken down into absorption.

untake of nutrients

• 1. transfer of nutrients into circulation
• 2. protects the body from harmful ingested material

• 1. reductions of particle size leading to an increase of surface material.
• 2. conversion of food to an isotonic aqueis solution.
• 3. solubilization (emulsification) of hydrophobic lipids
• 4. enzomatic digestion of large molecules to small fragments
• 5. absorbtion of small molecules of digestion across intestinal cell.

• same # of non-penetrating particles, cells will neither decrease
• -will not shrink or swell.

• mouth- mechanics break down and making saliva
• -things start to absorb in mouth under tongue

food that has been swolloed

once food is swallowed.

90% absorbtion occurs

absorbs water that is being reabsorbed

chiseled edes that cut

pointed crowns that tear.

ridged surfaces that crush and grind

way muscular contraction of gastro tract pushes things along.

• 1. circular
• 2. longitunital
• 3. diagonal
• -goal is to produce a mixture of use of them.

prevents air from getting into esophageal

between esophages and stomach prevent back juice in esophagest.

seperates the acidic from nutral enviroments it always only small amount of chyme

between small and large intest. prevents material from coming back in.

• tums
• rolex
• -form of calcium

• pepcid
• -reduce amount of stomach acid

Chronic inflammation and damage of the esophages

• salivary glands
• stomach
• pancrees
• liver (gallbladder)
• small intestint

• 99.5% water
• lubricationg the food

start to break down large stach molecules to mono and disacarides.

lipid enzyme involved with tryglycerides with short and mediam chain fatty acids.

• hydrochloric Acid (HCl)
• pepsinogen-->pepsin
• mucus`

• synthesis of hormones
• -glucagon and insolin

sythesis and sucreation of digestion enzyme.

97-99% water lubricate to get mixture.

• buffer acid that is coming out of stomach
• -stops pepcid from functioning

enzymes

dont want active till in form of food.

primary amylase that take carbons apart.

gong to cut last a.a. off.

bile

• no enzymes
• fat digestion

• 1. ammolsification of fat
• 2. contains bycarbonate to neutrilies acid
• 3. route of cholesterial excretion as well as bile acid

reabsorb water

primary absorber

tubular gland that lies between intestinel bili and screts intesten juices

• 3-5 days
• constently changing and moving

• simple diffusion
• facilitated diffusion
• active transport

things that can move simply in more right through (small lipids and water)

required a carrier. --> changes shape to go into cell. (vitamins)

• energy
• going agenst concentration gradient. (glucose and a.a.)

• Release enzymes
• contraction of muscles
• absorb nutrients

digest food.

lympatic system (do not go to liver first) go to rest of body.

quicker

slowely

• protective organ
• everything your body is trying to get out of system.

a group of compounds composed of carbon, oxygen, hydrogen, and nitrogen arranged into amino acids.

building blocks of protein

each contain an amino group, an acid group, a hydrogen atom, and a distinctive side group all attached to a central carbon.

they have different side chains on amino acids.

• differ in size, shape, electrical charge, and other characteristics which leads to different biological properties.
• this changes there function.

• 9
• histidine
• isoleucine
• leucine
• lysine
• methionine
• phenylalanine
• threonine
• tryptophan
• valine

• 11
• alanine
• arginine
• asparagine
• aspartic acid
• cysteine
• glutamic acid
• glutamine
• glycine
• proline
• serine
• tyrosine

• 5 a.a.
• all others are essential until pathways function right.

tyrosine

conditionally essential for them.

your diet

making it in your body.

beta amino acid containing a sulfonyl group.

• decrease growth
• neralogical
• blindness
• retinal degeneration

• animals
• they float in body as free amino acid.

• body but might not have enough so have to eat some.
• supplemented in all major infant formulas.

a.a. be used for energy but to do so the nitrogen needs to be removed for this process.

• chemical process that your body takes fat and carbs to make a.a.
• adding nitrogen group (NH3) to it makes it happen

• the bond that connects the acid end of one a.a. with the amino end of another, forming a link in a protein chain.
• - condenstation reaction

• one molecule to another making it from another a.a.
• Transform amino group (NH3) from amino acid to keto acid to form a new amino acid and new keto acid.

using other a.a.

a few dozen to several hundred.

protein

• di=2
• tri=3
• poly=4
• sequence of a.a. tells them what to do.

• uncoiling of a protein
• happens when you heat it up
• easier to digest

• gives different functions
• different structures let them do different things

• different side chains on different a.a. have various chemical properties
• -water to the inside forces twist and bend in the protein.

is not to provide specific body protein directly but to supply the a.a. from which the body can make its own proteins.

denatures protein activates pepsion.

break protein up to small units.

digestion-->AA-->absorption-->blood-->tissues--> make protein that we need.

deoxyribonucleic acid

Ribonucleic Acid

• DNA-->RNA
• step 1 of protein synthesis overview
• uncoil DNA and copy it to mRNA
• goes on in nucleous then leaves.

• you
• gene expression is protein expression.

• transfer RNA bring a.a to mRNA
• have to be in a certain order
• tells which one to site down.
• translating them into protein.
• hemogloben can't carry oxygen well.

facilitate actions in the body and sometimes they are just used.

protein that facilitate chemical reactions w/out being changed in the process.

• 1. break down substance
• 2. make a new substance
• 3. transform a substance into another

• most of bone and tissue
• building blocks protein in our tissue.

• chemical messengers not all hormones are protein but most are.
• tell certain part of the body to do something.

• control of fluid inside cell and outside of cell
• water goes were protein is

in cell

outside cell

between cells

with in blood vessels.

swelling

• 1. excessive protein due to kidney disease
• 2. inadiquit protein sithases due to protein
• 3. inadiquit protein intake

• acids release h ions to buffer
• protein w/ neg. charge accepts them

different proteins transport all sorts of things.

• anything you are exposed to that is not you.
• -body makes antibody that are protein.
• -these proteins allow you to have immunity

blood clotting

retna of eye (protein) when light hits protein it will change canfirmation ineshats sights

• protein can be used for energy
• can be used to provide energy and glucose.

constantly breaking down protein and have to make new ones.

in a healthy adult protein sythises equals degrigation and protein intake (dietary) equals nitrogen excrition in feces, sweat, urine

estimate of protein requirement.

zero nitrogen balance (equilibrium)

• positive nitrogen balance
• body senthesies moves protein then it degreades
• ex: pregnancy and growth (children)

• negative nitrogen balance
• body breaks down more protein then it makes.
• ex: some one starving

breaking proteins down out of essiential a.a.

a.a. tyrosine used to make neurotransmitters

• main way store energy- fat
• not bodies intent to store energy as protein
• when it is deprived of energy it will use this.
• -body will lose lean mass

• 1. does this provide proper balance of a.a. for body needs
• 2. is it digestable

• All essential a.a. must be provided at the sametime for protein sythesis to occur
• - 1 missing, a.a.= no protein

amino acids absorbs for a given protein intake.

• make all essintial amino acids needs in relavent to a human requires.
• ex: meat-red, fish, poultry

• two or more dietary protein that when put together you get all essential a.a.
• ex: beans and rice

• a standard protein that meets the essential a.a. requirements of preschool-age children
• -egg usually used

• compare protein in food to gold standard (egg)
• lower chemical score not as good for you.
• may not reflect the way the body will use protein.
• fails to take into account digestibility of a protein.

• like a.a. scoring
• takes into account digestibility

measures of efficiency of a protein to support the body's needs.

look back over pae 9 in notes

• measure weight gain in growing animals compared to its protein intake.
• growing animal- feed it source of protein if it grows good source if not can figure out why.
• nothing will go in baby food unless it goes through this.

not getting all nutritients they need.

• PEM caused be a recient event of food restriction
• -can tell by normal height thin for height

• long term food depervation
• -will be short for age

• if you don't have protein and can't make it you will die.
• no matter quality of calories not getting enough body will use protein for energy.

• Chronic PEM- lack in both energy and protein
• -defisiant in almost everything
• - impair muscle and brain development
• - running on very basis of living life
• - body not good at absorbing nutrients

• can not make lipoproteins that carry fat from the liver so you end up with a fatty liver.
• -no antibodies = increase infection
• -increase infection= increase kwashiorkor
• - other proteins decrease making them mroe suseptable to infection

• getting enough calorie but not enough protein
• -kids will have adema (swelling in abdominal area)

eat nothing to do with animal diet

eat milk based products

eat milk and eggs