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Nutrition Year 1 > Proteins > Flashcards

Proteins Flashcards

1
Q

how much of body weights proteins account for?

A

Protein 20%
Fat 10%
Water 65%
Minerals 4%
Carbs 1%

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2
Q

which chemist first discovered proteins in 1839?

A

Gerharld Mulder

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3
Q

what atoms make up a protein ?

A

Carbon
Hydrogen
Oxygen
Nitrogen

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4
Q

The presence of which atom distinguish proteins from carbs and fat?

A

Nitrogen

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5
Q

what are amino acids

A

the basic building blocks of proteins

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6
Q

what do amino acid contain?

A
  • 1 amine group - NH2
  • 1 carboxylic Group - COOH
  • 1 unique side group (R-group)
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7
Q

How many amino acids out of the 100 in nature do the human body require?

A

20 amino acids for protein synthesis

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8
Q

what is a protein and what is it made of? With which term can protein be interchanged with?

A

Proteins are Macromolecular polypeptides = large molecule made of many peptide-bonded amino acids
Polypeptide

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9
Q

what is so particular about the structure of the amino acid chain folding of a protein ?

A

The amino acids fold in a 3D structure linked to the function of the protein (lock and key)

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10
Q

give an example on a non-protein building block amino acid

A

Citrulline is a non-protein building block amino acid that plays a role in the urea cycle

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11
Q

which amino acids make up glutathione?

A

Cysteine - conditionally essential
Glutamic Acid - non-essential
Glycine - conditionally essential

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12
Q

How many amino acids are essential AA and name them

A

9 essential AA - PVT TIM HiLL
Phenylalanine
Valine
Threonine
Tryptophan - serotonin and melatonin
Isoleucine
Methionine - methyl donor
Histidine
Leucine
Lysine

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13
Q

what is a complete protein?

A

A protein that contains all the 9 EAAs (like animal protein and certain vegetarian proteins)

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14
Q

Which EAA is considered conditionally essential by some experts and why?

A

Histidine because it is synthesised in small amount by gut bacteria in adults and it does not impair protein synthesis when it is missing from the diet.

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15
Q

what causes protein denaturation? and Why a acid forming diet is problematic?

A

When exposed to heat, variation in pH, alcohol, heavy metals (aluminium)
=> lose its 3D structure, the protein unfold and lose its biological activity and function. They unravel.
Acid forming diet is problematic because it changed the pH around the cells and can impact the functioning of proteins within the cells

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16
Q

Why are protein denatured through digestion?

A

To facilitate the process of proteolysis which allow the protein to unfold for digestion of amino acids with the help of Pepsin enzymes

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17
Q

what is pepsin ideal pH

A

2 in the stomach

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18
Q

Name 3 function of proteins?

A
  • Structure of body tissues - collagen
  • Mouvement - Actin and myosin
  • Carrier molecule - Haemoglobin (bind to O2)
  • Storage molecule - Ferritin (bind to iron)
  • Fluid balance - Albumin (bind to calcium, zinc and B6, steroids and fatty acids)
  • Enzymes for reaction in the body - amylase
  • Hormones - insulin, thyroid hormone (tyrosine), dopamine (tyrosine), adrenaline (tyrosine), serotonin and melatonin (tryptophan)
  • Hormone receptors - cell membrane proteins are receptors for hormones
  • Immune functions - antibodies IgG (virus and bacteria), IgA (saliva, tears, mucous), IgM (first to appear in antigen exposure) and IgE (allergies)
  • Clotting mechanism - clotting factors
  • Alternative energy source
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19
Q

What are the 6 conditionally essential AA

A
  • Arginine
  • Cysteine - taurine
  • Glutamine - most abundant AA in the body
  • Glycine - glutathione
  • Proline
  • Tyrosine - Thyroid hormone, dopamine, noradrenaline, epinephrine
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20
Q

what is the best buffer amino acid to regulate the acid/base balance and why

A

Histidine because can easily pick up and let go of H+ ions
Cysteine as well

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21
Q

give 3 protein related causes of oedema

A

kidney disease - protein loss
liver disease - inadequate protein synthesis
protein malnutrition - ascites (water more in peritoneal cavity)

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22
Q

What are glycoproteins? name 3

A

Glycoprotein are a protein bound to a sugar

  • Mucins = in mucous and saliva
  • ABO blood type antigens
  • LH and FSH and TSH
  • Major Histocompatibility Complex - antigen presentation
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23
Q

Describe & explain the 3 step process of protein metabolism

A

Protein metabolism = when we need to use protein for fuel or to convert protein into fat storage
Excessive protein from food will be transformed into energy

3 steps:
1. DEAMINATION - removal of the amine group
2. UREA CYCLE - conversion of ammonia formed during deamination to urea for safe removal
3. TRANSAMINATION - redistribution of AAs

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24
Q

Explain the process of Deamination in protein metabolism

A

1st step of protein metabolism

Removal of the nitrogen-containing amine group
Takes place in the liver
Purpose = for individual amino acids to be used as energy source or stored as fat

After deamination, the remaining fragment of amino acid can be used to produce glucose or ketones

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25
Q

Explain the urea cycle in protein metabolism

A

2nd step after deamination

Ammonia is formed during deamination and needs to be converted to urea for safe removal from the body by the kidney (urine)
Takes place in liver cells (hepatocytes)
Hepatocytes convert ammonia in urea (a water soluble compound)

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26
Q

what is hyperammonaemia and what are the signs and symptoms?

A

Hyperammonaemia is elevated ammonia in the blood when the urea cycle is impaired
Signs and symptoms:
- Chronic fatigue
- nausea and diarrhoea
- irritability
- poor concentration and confusion
- headache
- intolerance to high protein food

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27
Q

Explain the transamination in protein metabolism

A

Essential in the synthesis of some non-essential AA
Redistribution of AA. If a non essential AA is not available, body make it from another
AA+keto acid <=> AA+keto acid
Transaminase co factor is B6

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28
Q

What is protein turnover?

A

Protein in the body are continually made and broken down
example = enzymes may be recycled in minutes

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29
Q

which vitamin is a cofactor of transamination?

A

B6

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30
Q

what is the amino acid pool?

A

When proteins breakdown they free amino acids to join circulation = the amino acid pool = group of amino acids that stay in circulation for a period of time and are not stored
These amino acids will be then be utilised or excreted

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31
Q

how long do amino acids in the amino acid pool stay in circulation for?

A

EEA have a longer half life than non-EAAs

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32
Q

Why is it important to have a regular supply of protein in the diet?

A

Because amino acids stay in circulation for a short period of time and if they are not used they are excreted (not stored).

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33
Q

What happen if the amino acid pool does not contain the EAA the body needs?

A

The body will start to break down its own tissues to obtain EAA not in the current poll => muscle loss.

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34
Q

what is the impact of stress on skeletal muscles?

A

Stress causes protein loss in skeletal muscles due to the catabolic action of stress hormones
on going stress can impact collagen in the bones matrix => osteoporosis

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35
Q

What are protein sources? What food do not have proteins?

A

Whole food - even fruits
Abundant sources of protein include - legumes, nuts and seeds, greens, whole grains, eggs, fish, poultry and meat.
Processed food do not have protein

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36
Q

how much protein a day does the human body reabsorb from shed mucosal cell? How do you call these sources of protein?

A

50g/day of protein
Endogenous sources of protein

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37
Q

what is the issue with animal protein sources?

A

They require more energy to digest and can accumulate in the the intestinal wall impairing absorption.

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38
Q

what determine protein quality?

A

digestibility and amino acid composition

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39
Q

how do plant and animal protein digestibility varies?

A

gut function (HCl and digestive enzymes)
fibres presence
anti-nutrient factors in plant food (phytates and lectins)

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40
Q

How can you improve the digestibility of plant protein?

A

soak, sprout, ferment => can lower anti nutrient factors like lectins and phytates

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41
Q

why are plant proteins a superior choice to animal protein?

A

Because they contain fibres, phytonutrients, vitamins and minerals

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42
Q

How to optimise protein digestion?

A
  • chew
  • no water with meal
  • support stomach acid levels:
    => zinc and B6 rich foods
    => ACV
    => Bitter herbs and foods before meals (dandelion, rockets, watercress, artichoke, gentian, barbers bark, goldenseal)
    => Betaine hydrochloride supplements 600mg per capsule - start with one at the beginning of a meal before increasing ti max 5
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43
Q

B6 rich foods

A

whole grain, dark leafy green, banana, carrots, potatoes, sunflower seeds, walnuts, avocado, pulses and beans, lentils

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44
Q

zinc rich food

A

pumkin seeds, nuts

45
Q

what happen to undigested protein that reach the colon?

A

it is fermented creating toxic metabolites that increase the inflammatory response and encourages the proliferation of opportunistic pathogens => E.coli

The fermentation products of protein (ammonia, amines, sulphides, n-nitroso compounds) are detrimental to health ==> effect include systemic toxicity, carcinogenesis

46
Q

How can you avoid protein fermentation in the colon?

A

Eat plenty of fibres + plant protein to promote a better pathway of fermentation in the colon

Optimising protein digestion is crucial to ensure as little as possible reach the colon undigested

=> non protein overload
=> make sure the protein is well digest
=> ensure protein quality

47
Q

what is a limiting amino acid in a plant protein source? which one are they?

A

If an EAA is supplied in less than the amount needed to support protein synthesis in a plant protein source it is called a limiting AA.

The limiting AA lysine, threonine, methionine and tryptophan ==> they are found in shortest supply in incomplete proteins

you need to rotate protein sources to provide balance

48
Q

what is the limiting AA of the following food?
Beans, grains, nuts & seeds, vegetables, corn

A

Beans = methionine
Grain = lysine and threonine
nuts & seeds = lysine
vegetables = methionine
corn = tryptophan and lysine

49
Q

What are the vegan food that are complete protein (contain all 9 AA?)

A

quinoa
buckwheat
tempeh
pumpkin seeds
chia seeds
hemp seeds

50
Q

How to combine incomplete protein to ensure all EAAs are obtained?
Beans, grains, nuts and seeds, vegetables and corn

A

Beans (methionine) + grains/nuts and seeds
Grains (lysine, threonine) + beans
nuts and seeds (lysine) + beans
Vegetables (methionine) + grain/nuts and seeds
Corn (tryptophan, lysine) + beans

51
Q

what are the negative effects of high animal protein diets? Which amino acid is highly abundant in animal protein?

A
  • Methionine is highly abundant in animal protein and has an immune stimulating effect on T-cells which in excess is associated with an over reactive immune response (autoimmunity and chronic inflammation)

Excess methionine also increase homocysteine associated with atherosclerosis

  • unless organic, meat can leave chemical reside from crop they eat
52
Q

what are the 6 adverse effect of excess protein?

A
  1. osteoporosis = the acidic burden of excess animal protein can draw calcium out of the bones because of body buffer system, but a protein deficiency will also affect the bones because we need protein for the collagen structure
  2. kidney disease = the extra acidity need buffering from the kidney
  3. increased cancer risk = both high and moderate intake of animal protein increases cancer risk especially processed meat which are carcinogenic
  4. disorder of liver function
  5. atherosclerosis = excess protein is associated with oxidation and inflammation of the endotheliallium
  6. increased muscle soreness post exercice => animal protein is acidifying
53
Q

what is considered a high protein intake ?

A

20% of total calorie intake or more

54
Q

how can you balance the acidity of a high animal protein meal?

A

with fruit and vegetables which are alkaline

55
Q

protective effect of plant based protein?

A

peas, legumes, wholegrain, nuts and vegetables => fibre, phytonutrients and prebiotics

Lower levels of methionine
Lower levels of leucine (increase the expression of TOR enzymes that regulate cell growth)

56
Q

How much protein to be at risk of protein deficiency?

A

0.4-0.5g/kg body weight

57
Q

general recommendation of protein intake per kg of body weight? recommandation for athletes?
for pregnant women how much would you add?

A

General - 0.75g / kg body weight
Minimum activity - 1.0g/ kg body weight
Moderate activity - 1.3g / kg body weight
Intense physical activity - 1.6g / kg body weight

But the increased need for protein for athlete is likely to be met by the increase of required calories

For pregnant woman add 6g/day to 0.75g/kg body weight
Lactation +11g/day 0-6month and +8g/day 6+ months

1g/kg body weight for vegetarian and vegan to accommodate for the lower protein bioavailability

58
Q

Which category of people is most likely to be affected by protein deficiency?

A
  • children - high sugar diet and low whole foods
  • teenagers - dieting, junk food
  • older people - poor chewing, digestive health issues (lower HCl), living situation
  • anorexia
  • recovering patients post surgery or post trauma

In developed world it is most likely to affect:
- homeless
- drug and alcohol addicts
- those with chronic digestive conditions or chronic PPI users
- those with chronic infection

59
Q

what else amino acids are used for apart for protein synthesis?

A
  • Synthesis of hormones and neurotransmitters
  • Neurotransmitters themselves (glycine)
  • Methyl donor (methionine)
  • Build bile acid for digestion (taurine and glycine)
  • Precursor for NO production (Arginine)
  • Help detox chemicals in phase II liver detox
  • Precursor to endogenous antioxidant like Glutathione (glycine, cysteine and glutamine
60
Q

How can you assess the amino acid profile of a client? for which client would you use that?

A

Urine or plasma samples
Chronic use of PPI, Chronic Fatigue Syndrome

61
Q

why can an oedema occur when protein level is too low?

A

because albumin is a protein that regulate water retention in the blood. If not enough albumin, water is released in body tissue interstitial spaces

62
Q

What is GLUTAMINE - conditionally EAA?
What does it fuel?
Why is it conditionally EAA?

A

Glutamine is the most abundant AA in the body
It is the preferred fuel of rapidly dividing cells (enterocytes, lymphocytes and macrophages)
Body glutamine synthesis requirement can’t be met in acute stress period (injury, infections)

63
Q

What is the effect of glutamine on the intestinal barrier?

A

Glutamine is AA source of intestinal cells and help regulate tight junctions integrity => leakage of LPS in blood which can lead to various chronic disease

64
Q

How to increase intestinal permeability?

A
  1. Glutamine supplement - 10/day in divided doses
  2. Glutamine rich food - cabbage juice (1L fresh juice for 10 days), spirulina, asparagus, broccoli, cod, salmon
  3. N-acetyl glucosamine in shellfish
  4. Quercetin (red apples, red onions, tomatoes, red peppers) - anti inflammatory and antioxidant
  5. Zinc - rapid cell division support
  6. anti oxidant like vit C and E and beta carotene
  7. Turmeric, marshmallow, slippery Elm, Goldenseal, Myrrh
  8. Bone broth (rich in collagen and glucosamine, chondroitin, glycine)
65
Q

Name 5 functions of Glutamine

A
  1. GIT tight junction - increase intestinal permeability
  2. Immunity - supports lymphocytes and macrophages proliferation
  3. Hypoglycaemia - glutamine is a substrate for glycogenesis (2tsp with water between meals instead of a snack while adapting to healthier eating)
  4. Muscle recovery - improve recovery
  5. Neurotransmitter - Glutamine => glutamate (excitatory) => GABA (inhibitory) - the conversion from glutamine to GABA requires Taurine and B6 and Zinc => relieve anxiety and stress and support sleep

HIV support - 30g glutamine/day - chronic infection so the body uses more glutamine

66
Q

Glutamine food sources

A
  1. fish and shellfish (Sardines, mackerel, crab, lobster, shrimps and prawns are all good sources) - 50g of mackerel contains just under 2000mg of glutamine, that’s around 1.9g
  2. Red cabbage - 100g red cabbage contains around 300mg, or 0.3g of glutamine
  3. Dairy
  4. Egg - 1 large egg contains 0.8g of glutamine
  5. Nuts and Seeds - A large 50g handful of cashew nuts contains around 2.2g glutamine
  6. Dark leafy greens - Parsley contains 1.8g glutamine per 50g
  7. Soya
  8. Red kidney beans - 0.6g glutamine per 100g

Meat is one of the most rich in glutamine foods.

Roast chicken, for instance, contains around 5.5g of glutamine per 128g portion

67
Q

what vitamins and minerals are required for glutamine conversion to GABA?

A

zinc B6 and taurine

68
Q

Glutamine supplementation dosage ?

A

Start low and increase 1-30g/day (in am)

69
Q

Glutamine supplement drug interaction and toxicity

A

Interaction with anti seizure medication

No adverse effect

Caution = cancer cells use glutamine for fuel, avoid with epilepsy and with kidney disease to relieve AA load on kidney

70
Q

What is Cysteine - conditionally essential AA ?

A

Cysteine is a sulphur containing AA formed from Methionine and Serine in the Liver (with B6, B9 and B12 as co-factors)

It is a component of glutathione and is needed for Co enzyme A and taurine

Cysteine is a rate limiting AA for glutathione = if there is a limited amount of cysteine the body will produce the min amount of glutathione and keep the cysteine for other uses

Cysteine contains sulphur = used in phase II liver detox pathway sulfation

71
Q

What co factors are required to form cysteine from methionine and serine?

A

Vitamins B6, B9 and B12

72
Q

Cysteine food sources

A

legumes, sunflower seeds, eggs and chicken

73
Q

What does it means Cysteine is a rate limiting AA for glutathion?

A

Cysteine is a rate limiting AA for glutathione = if there is a limited amount of cysteine the body will produce the min amount of glutathione and keep the cysteine for other uses

74
Q

N-Acetyl cysteine functions x4?

A

Liver detox = Crucial in drug metabolism in liver (drug deplete glutathione and cysteine regenerates it)
Antioxidant = building block of glutathione
Reproductive health = increase sperm concentration due to its antioxidant properties - impact serum testosterone positively
Respiratory health = breaks up mucus and helps eliminate it from respiratory tract
Insuline resistance = help improve insuline sensitivity

Increase paracetamol detox in the liver - paracetamol is detoxified using the glutathione pathway

In HIV patient who are depleted in glutathione
In neurodegenerative diseases where oxidative stress is s big factor

75
Q

N-Acetyl cysteine dosage and drug interactions and caution

A

600mg-1500mg/day
Interaction with insulin use and nitro-glycerine
Can cause GI adverse effects

76
Q

What is Methionine - EAA - what is its major function?

A

Methionine is a sulphur containing EAA => major methyl donor (in homocysteine cycle and phase II liver detox)
Too much methionine is linked to increase cancer risk and exacerbated ageing BUT raised homocysteine is linked to atherosclerosis, and miscarriage risks

=> use B6, folate and B12 to support methylation and restrict dietary methionine to lower homocysteine

77
Q

What is Carnitine (methionine + lysine) ?

A

Carnitine is an AA derivative synthesised from methionine and lysin. This production requires iron, vit C, B3 and B6

Deficiency is rare BUT mutation of SLC22A5 gene can make it a conditionally EAA.

78
Q

Carnitine direct food source?

A

nuts, seeds, avocado, asparagus, spinach and red meat and dairy

79
Q

What is the link between carnitine and the thyroid hormone?

A

Carnitine is a peripheral thyroid hormone antagonist = inhibits the physiological action of thyroid (can be used in hyperthyroidism but counter indicated for someone with hypothyroidism)

80
Q

What is carnitine main function?

A

Assists ATP production from fatty acids = facilitates the transport of Long chain fatty acids across the mitochondrial membrane so they can be oxidised to create ATP.

Also an antioxidant in mitochondria.

Helpful for fat loss, infertility, fatigue ad concentration, athletic performance and ADHD (increase dopamine and acetylcholine production)

81
Q

carnitine supplementation dosage and drug interaction

A

2-4g/ days divided dose => but much better absorption from food than from supplement

Interaction with warfarin (blood thinning) and thyroid hormone as a peripheral thyroid hormone antagonist

Caution: nausea, lose bowel, vomiting, abdominal cramp, heartburn => can cause urine ans breath to have a fishy smell

82
Q

What is creatine and what is it made from?
Where is it formed ?
Where can it be found in body?
What is its main function?

A

Creatine is a small peptide made from Arginine, Glycine and Methionine

It is formed in the liver

Found 95% in the muscles (+ brain) => fast source of ATP in the form of creatine phosphate

83
Q

Creatine direct food source?

A

meat, fish and eggs

84
Q

Creatine main function?

A

A storage form of ATP = enables explosive power in the muscles for 8-12 seconds
Enhance muscular activity (skeletal and cardiac - can be used in heart failure and coronary heart disease)

85
Q

Creatine supplementation dosage and drug interaction

A

Skeletal muscle can reach saturation point with creatine in the first few days of loading => if a weight trainer supplement 20g for 5 days, it would have to reduce to 0.3g/kg of body weight then.

combining creatine with caffeine may lead to ischeamic stroke
High dose of creatine might affect renal function

Can cause abdominal pain, nausea, palpitation and muscle cramp - draw water into the muscle causing weight gain

86
Q

What is Glycine used for? - Conditionally EAA
Co-factor in the synthesis of glycine?

A

Glycine is a conditionally EAA used in the case of certain metabolic stresses:
- increase haem synthesis for blood formation
- collagen formation fro growth and repair
- glycine conjugation in detoxification

Made with the help of serine and B6

87
Q

glycine food sources?

A

legumes, kale, cauliflower, cabbage, banana, pumpkin, bon broth, meat and fish and eggs

88
Q

Glycine 3 functions?

A
  1. collagen synthesis = collagen isn the most abundant protein in the body and is 1/3 glycine (crucial for GIT repair, skin and MSK integrity)
  2. Liver detox - required to conjugate toxins in phase II liver detox
    => constituant of glutathione and bile acid
  3. Neuro transmitter => inhibitory neurotransmitter in the CNS
    also can reversely convert to serine to form acetylcholine => insomnia, learning and cognition, CALMING
89
Q

What is Taurine synthesised from (AA) ?
When does it need to be supplemented?

A

Taurine is synthesised from cysteine with the help of B6

Need to be supplemented in case of extreme illness or stress
Need to be supplemented to non-breastfed infants

90
Q

Taurine direct food sources?

A

Only animal (chicken and turkey)
For vegans and vege => increase cysteine and B6 intake

91
Q

Taurine 5x main functions

A

Muscle health - play a role in contraction. improve heart muscle health

Antioxidant - protects mitochondria from ROS (good for atherosclerosis and infertility sperm health)

Neurological health - taurine is an agonist of GABA receptors in CNS = CALMING.
Neuroprotective

Bile production - better flow from liver when taurine

Insulin resistance

92
Q

Taurine supplementation and interaction?

A

Dosage = 500mg 3x/day
Drug interaction with lithium for bipolar disorders can worsen symptoms

Safe up to 6g a day

93
Q

what is Theanine and what is it used for ? Where is it uniquely found?

A

Theanine is a non-essential AA
Theanine is uniquely found in green tea
Theanine reduces the negative effects of caffeine naturally in green tea by having opposing effects (relaxing rather than stimulating)
Theanine is considered therapeutic in Ayurveric medicine due to its balancing effects especially for those who are restless and anxious

94
Q

Theanine main function?

A

Neurological (calming)
- After ingestion, thiamine crosses the blood brain barrier and blocks glutamate receptors whilst increasing GABA activity. GABA is inhibitory / calming
- mood-enhancing effect without drowsiness
- increase dopamine and serotonin

=> studying/concentration, anxiety, stress, insomnia, low mood, hypertension

95
Q

Theanine supplementation dosage / interaction / adverse effect

A

Dose - therapeutic dose = 50-200mg/day (green tea is to a practical source)
Drug interaction = can lower blood pressure
Can cause headache and sleepiness

96
Q

What is Tyrosine derived from - Conditionally EAA

A

Tyrosine is derived from phenylalanine (EAA)
Tyrosine may become conditionally EAA is high stress because conversion from phenylalanine to tyrosine will be reduces

97
Q

Tyrosine food sources

A

nuts, seeds, legumes, whole grain (quinoa and oats), fish meat and poultry (widely available)

98
Q

Tyrosine main function? and therapeutic uses

A

Endocrine health = tyrosine is a precursor for thyroid hormone, dopamine, epinephrine and norepinephrine and melanin

-> adrenal fatigue
-> hypothyroidism
-> ADHD
-> Depression
-> Anxiety
-> Cognition

99
Q

Tyrosine supplementation and dosage / interactions / cautions

A

Dosage = 400-6000mg/day tyrosine seems to be safe
Drug interactions = MAOI antidepressants / thyroxine medication / Levodopa in Parkinson’s
Contraindicated in overactive thyroid and melanoma
High dose can cause GIT upset

100
Q

Tryptophan - EAA - food sources

A

brown rice, quinoa, pumpkin seeds, oats, banana, turkey, fish, eggs

101
Q

Tryptophan 2 functions and therapeutic uses

A
  1. Endocrine health
    - Used for serotonin and melatonin synthesis
    - Consume supplement with a carb rich snack as tryptophan need insulin to cross the BBB
    - Low level of serotonin lead to carbs cravings
    => depression, insomnia, stress and anxiety, PMS< migraines, weight control (cravings), overcoming smoking addiction
  2. ATP synthesis
    - Tryptophan is used to make B3 which is needed for NAD and NADP coenzymes in ATP production
    => fatigue, fibromyalgia, Alzheimer’s
102
Q

Tryptophan pathway

A

tryptophan => 5-HTP => serotonin => melatonin
tryptophan => B3
Tryptophan => protein synthesis

103
Q

tryptophan supplementation dosage / drug interaction / adverse effects

A

Dosage = 100-600mg/day (5-HTP usually preferred)
Drug interaction = antidepressants, sedative, tramadol
Adverse effect = L-tryptophan can cause heartburn, abdominal pain, flatulence, nausea, vomiting and diarrhoea, loss appetite

104
Q

Phenylalanine (EAA) food sources

A

avocado, brown rice, lentils, eggs, fish, meat and soy

105
Q

Phenylalanine 2 functions and therapeutic uses

A
  1. endocrine health = phenylalanine can be converted to tyrosine
    => thyroid health, cognition, depression
  2. skin pigmentation => melanin production via the tyrosine pathway
    => vitiligo 50-100mg/kg for 6-18months
106
Q

Phenylalanine dosage

A

150-7000mg/day
can worsen schizophrenia symptoms

107
Q

Lysine dietary sources (EAA) - which AA does it compete with for absorption?

A

Lysine is the sister amino of Arginine and compete for absorption
- Lysine dietary sources = quinoa, legumes, tempeh, chicken, eggs dairy, fish and red meat
- Arginine dietary sources = nuts, seeds, seaweeds, meat => avoid when you have herpes (virus uses arginine to replicate)

108
Q

Lysine key therapeutic uses x4
Dosage

A
  1. Cold sores (herpes simplex virus) = more effective when supplemented with vit C
  2. Collegen = lysine is part of collagen helps build muscular tissue
    => Muscle injury recovery, osteoporosis
  3. GIT Absorption of zinc, calcium and iron
    => osteoporosis, hair loss, anaemia
  4. Glucose lowering effects => hyperglycaemia and diabetes

Dosage = 300-3000mg/day

Nutrition Year 1 (10 decks)

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