(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
Vit A deffiency
Night blindness, xerophthalmia
26
Vit K deffiency
defective blood coagulation
27
Vit E deffiency
musclar dystrophy
28
Vit D deffiency
rickets
29
Oral Chenodeoxycholic acid
used to help desolve galstones
30
Disulfide bonds
oxidation of SH group on cysteine residues in the lumen of the rough ER
31
Keratin has a high ______. If you manipulate this what happens?
cystine content and will tend to form disuflide bonds. -mainpualting the bonds is the key to curling or straghiening hair`