9. Proteins Flashcards

1
Q

Essential Amino Acid vs. Limiting Amino Acid

A
  • essential amino acids are required because body can’t make them on its own
  • limiting amino acids
    one of the essential amino acids is lacking in quantity to support growth of protein
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2
Q

Complete Protein

A

contains every amino acid in sufficient quantities (animal sources contain all essential amino acids while plants are lacking in some)

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3
Q

How is the quality of a protein determined?

A

By evaluating a protein based on requirements of the human body and their ability to digest it

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4
Q

What is the role of stomach acid in protein digestion?

A

Stomach acid activates pepsin and denatures the proteins

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5
Q

Endopeptidase vs. Exopeptidase

A
  • endopeptidase breaks bonds within the polypeptide chain

- exopeptidase breaks the bonds at the end of the chain

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6
Q

How are amino acids absorbed?

A

They’re absorbed in the small intestine via energy dependent transport carriers through a concentration gradient

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7
Q

How can dietary overload of non-essential amino acids cause a deficiency in an essential amino acid?

A

Amino acid absorption transport systems are shared

one amino acid may have priority over another which then causes the deficiency

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8
Q

Transamination vs. Deamination

A

Transamination
- reaction between an amine with an amino group and a keto acid with a keto group (amino acid becomes a keto acid and keto acid becomes amino acid)

Deamination
- causes the loss of the amine group from the amino acid which is replaced with a ketone

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9
Q

Amino Acid Oxidation

A

enzymes remove the amino group, leaving a carbon skeleton which is then broken down into acetyl-CoA and pyruvate

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10
Q

How does amino oxidation function with regard to neurotransmission?

A
  • many amino acids play roles as neurotransmitters
  • amino acid oxidation is one way (amino acids are converted into neurotransmitters)

Ex: oxidation of phynylalanine to form tyrosine

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11
Q

How does the body dispose of excess ammnia? Where does this occur?

A
  • the body turns ammonia into urea and excretes it in the urine
  • urea is made in the liver and kidneys from ammonia produced in the mitochondria
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12
Q

How are amino acids used for energy (where do they enter the energy production cycle)?

A

amino acids are broken down to Acetyl-CoA and pyruvate and then enter the krebs cycle

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13
Q

Ketogenic vs. Glucogenic amino acids

A

Ketogenic amino acids (degraded into acetoacetate)

Glucogenic amino acids (degraded into precursurs to gluconeogenesis and may be formed into glucose)

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14
Q

How does glutamine contribute to the synthesis of the nucleic acid bases?

A

Glutamine contributes to the synthesis of the nucleic acid bases because it is a precursor to the purine and pyrimidine nucleotide bases used in the synthesis of RNA and DNA

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15
Q

major routes of nitrogen loss from the body

A

nitrogen is lost as ureo in urine when glutamate gets converted to glutamine

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16
Q

Nitrogen balance

A

the amount of protein or nitrogen required by a human

  • the body is in balance (amount taken in = amount excreted)
  • the amount of nitrogen lost in urine, sweat, and feces is subtracted from the total amount taken in
17
Q

WHO protein recommendations

A
  • they’re derived by taking the digestibility of the protein and multiplying it by the amount of protein a person of a specific age group is supposed to consume
  • allows type of protein to be taken into account when finding the total mass of protein as a minimum the person must consume
18
Q

Potential complications from excess protein consumption

A
  • deficiency in an essential amino acid
  • renal stress
    increased incidence of colon cancer and obesity
19
Q

Kwashiorkor vs. Marasmus

A

Kwashiorkor - malnutrition causing the stomach to bloat (caused by insufficient protein intake with sufficient calorie intake)

Marasmus - inadequate energy intake in all forms (causes tissue and muscle wasting)

20
Q

20 major amino acids

A

Essential:
phynylalanine, tryptophan, valine, leucine, isoleucine, methionine, lysine, histidine, threonine

Non-Essential:
tyrosine, glycine, alanine, aspartate, glutamate, glutamine, asparagine, proline, arginine, serine, cysteine