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SFM > (DSA1) Biomolecules > Flashcards

(DSA1) Biomolecules Flashcards

1
Q

What are the fasting and fed blood glucose levels that are normal or indicative of hypoglycemia or diabetes mellitus?

DSA1 S5 LO1a

A

Normal:

  • fasting 70-100mg/dL
  • fed <140mg/dL

Hypoglcemia:
-<60mg/dL

Diabetes mellitus:

  • fasting >126mg/dL
  • fed >199mg/dL
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2
Q

What is the clinical significance of sugar alcohols and what are examples of these?

DSA1 S9 LO1a

A

Also referred to as sweeteners.

Significance:

  • poorly absorbed
  • low calorie
  • don’t contribute to tooth decay

Examples:

  • erythritol
  • xylitol
  • mannitol
  • sorbitol
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3
Q

What is the cause of lactose intolerance?

DSA1 S3 LO1a

A

Deficiency of lactase which leads to inability to digest lactose.

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4
Q

What are FA made from?

A

A-CoA

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5
Q

What are Isoprenoids?

DSA1 S17 LO1b

A

Structures derived from IPP (isopentenyl phyophosphate) which is itself derived from acetyl CoA.

Examples include:

  • steroids
  • lipid-soluble vitamins (A, D, E, and K)
  • CoQ
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6
Q

How are gallstones formed?

DSA1 S18 LO1b

A

Excess cholesterol and insufficient bile salt resulting in crystallization. Can lead to malabsorption (steatorrhea) and fat soluble vit deficiencies.

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7
Q

What are the nonpolar amino acids?

DSA1 S21 LO1c

A

GAPVIL MWF

  • glycine
  • alanine
  • proline
  • valine
  • isoleucine
  • leucine
  • methionine
  • tryptophan
  • phenylalanine
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8
Q

What are the polar amino acids?

DSA1 S21 LO1c

A

QT SYNC

  • glutamine
  • threonine
  • serine
  • tyrosine
  • asparagine
  • cysteine
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9
Q

What are the negatively charged (acidic) amino acids?

DSA1 S21 LO1c

A
  • aspartic acid (D)

- glutamic acid (E)

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10
Q

What are the positively charged amino acids?

DSA1 S21 LO1c

A
  • arginine (R)
  • histidine (H)
  • lysine (L)
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11
Q

What is the daily protein turnover of the average adult?

DSA1 S21 LO1c

A

Postive:

  • consumption ~100g
  • production ~400g

Negative:

  • degradation ~400
  • production of amino acid derivatives ~30g
  • excretion (variable)
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12
Q

How are disulfide bonds formed?

What are the nonpolar amino acids?

DSA1 S21 LO1c

A

Oxidation of sulfhydryl groups of AA cysteine resulting in a bond forming between the sulfurs of two cysteine residues

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13
Q

Glycogen

A

linear chain with alpha 1-4 linakges and branch points with alpha 1,6 linkages

  • food storage in animals
  • branching at 6-10 glucose
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14
Q

Starch

A

NOT FOUND IN HUMANS

amylopectin (75%) linear chains with alpha 1-4 linkages and branch points with alpha 1,6 linkages

  • branging 12-20 glucose
    amylose: 25% linear chains with alpha 1,4 linkages (no branching)
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15
Q

What degrades strach

A

alpha amylase

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16
Q

Cellulose

A

linerar chains with beta 1-4 linkages (degreaded by cellulase)

17
Q

What is ertythrose and what is it used in?

A

-4c tetrose, it is a PPP intermediate

18
Q

Sucrose

A

found in fruits and veggies

-diassacharide of glucose + fructose (alpha 1, beta 2 bond)

19
Q

Lactose

A

galactose glucose, beta 1-4 bond

20
Q

maltose

A

glu, glu alpha 1-4 bond

21
Q

What form of carbs do glycolipids and proteins use?

A

oligosaccarides (3-10 length)

22
Q

What are acetylated AA

A

COMPONENTS of glycoproteins and glycolipids (used in cell singaling, cell adehsion, immuno response)

23
Q

What are the 4 dietary lipids

A

-FA, TAGs, Cholestrol esters, phospholipids

24
Q

FA formula

A

CH3(CH3)n(COOH)

25
Q

Vit A deffiency

A

Night blindness, xerophthalmia

26
Q

Vit K deffiency

A

defective blood coagulation

27
Q

Vit E deffiency

A

musclar dystrophy

28
Q

Vit D deffiency

A

rickets

29
Q

Oral Chenodeoxycholic acid

A

used to help desolve galstones

30
Q

Disulfide bonds

A

oxidation of SH group on cysteine residues in the lumen of the rough ER

31
Q

Keratin has a high ______. If you manipulate this what happens?

A

cystine content and will tend to form disuflide bonds.

-mainpualting the bonds is the key to curling or straghiening hair`

SFM (31 decks)

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