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CLS 307 > Lecture 6 Chapter 7 > Flashcards

Lecture 6 Chapter 7 Flashcards

1
Q

What percent of urobilinogen get reabsorbed into blood

A

10-20%

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2
Q

What is albumin?

A

A carrier molecule

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3
Q

What happens when bilirubin is delivered to plasma and binds to albumin

A

Albumin carries hydrophobic molecule in blood until it gets to the liver

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4
Q

What happens once bilirubin reaches the liver

A

In the liver, the cells are hepatisized and separate bilirubin from albumin. Then they process bilirubin by adding 2 glucuronic acids

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5
Q

How does glucuronic acid help bilirubin

A

It makes it hydrophilic, now water soluble, and gives it charge. It is then added to bile

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6
Q

What happens once bilirubin reaches the bile?

A

Bile goes to the duodenum and bacteria starts breaking down bilirubin converting it to urobilinogen

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7
Q

What happens once bilirubin becomes urobilinogen

A

Travels down the intestinal tract. Some gets broken down to stercobilin, some gets reabsorbed into blood, and the rest travels to hepatic portal vein to liver

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8
Q

What happens after urobilinogen reaches the liver

A

Liver removes some urobilinogen and what’s left goes to the kidneys and gets filtered

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9
Q

What is stercobilin responsible for

A

Color of feces

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10
Q

What is urobilin responsible for

A

Pigment/color of urine

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11
Q

What does the prefix heme- mean

A

Iron

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12
Q

What does the suffix -globin mean

A

Protein

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13
Q

What is hemoglobin composed of

A

Iron
Protoporphyn IX
Protein

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14
Q

What is protoporphyrin

A

Heme that carries a central ferrous ion (Fe^2+)

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15
Q

What makes up a primary protein structure

A

A sequence of a chain of amino acids

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16
Q

What makes up a secondary protein structure and name those structures

A

Occurs when the sequence of amino acids are linked by hydrogen bonds
Alpha helix
Beta sheets

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17
Q

What makes up a tertiary protein structure

A

Occurs when certain attractions are present between alpha helices and beta sheets

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18
Q

What makes up a quaternary protein structure

A

It is a protein consisting of more than one amino acid chain

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19
Q

How can the biosynthesis of hemoglobin change

A

Can change based on the body’s needs

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20
Q

What are the 3 types of normal hemoglobin

A

Hgb A
Hgb A2
Hgb F

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21
Q

What makes up Hgb A

A

2 alpha
2 beta

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22
Q

What makes up Hgb A2

A

2 alpha
2 delta

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23
Q

What makes up Hgb F

A

2 alpha
2 gamma
(Only about 1-2% fetal)

24
Q

When a child is born what is their primary Hgb

A

Fetal Hgb (Hgb F)

25
Q

Name the 4 intrauterine Hgbs

A

Gower - 1
Gower - 2
Portland
Hgb F

26
Q

What makes up Portland Hgb and when is it present

A

2 Xi
2 gamma
1st 8 weeks of intrauterine life

27
Q

What makes up Gower 1 Hgb

A

2 Xi
2 epsilon

28
Q

What makes up Gower 2 Hgb

A

2 alpha
2 epsilon

29
Q

What makes up the abnormal Hgb H and why

A

4 beta
It will bind to itself if there is not enough alpha

30
Q

What makes up the abnormal Hgb Bart’s and what is the result

A

4 gamma
If there is no alpha at all, the child will not survive

31
Q

What is Hgb A1c and what percent of it is found in adult Hgb

A

Glycohemoglobin
Hgb with glucose attached/binded
4-6%

32
Q

If glycohemoglobin is lower than normal, what does that tell you

A

Something is wrong with the longevity of RBCs where they are being destroyed too early (anemia)

33
Q

What can Hgb A1c tell us?

A

Diabetes
Gives us an idea about the patient’s diet
With an increase in glucose in blood, it will be present in urine

34
Q

How does CO2 travel from tissue to lungs

A

CO2 combines with water and becomes an ion to transport. Once it reaches the lungs it dissociates and reverts back to CO2

35
Q

What percent of CO2 can dissolve

A

20-30%

36
Q

What is the normal pH

A

7.35-7.45

37
Q

What pH is wanted in your tissues

A

7.35

38
Q

How does O2 get released from Hgb

A

Hgb has 4 parts to it
H+ squeezes O2 out of each 4
The first H+ requires a lot of energy
The second H+ requires less energy
The third H+ is very easy
Don’t even need a 4th H+

39
Q

On an oxygen dissociation curve, how do you push the graph to facilitate Hgb to let go of O2

A

Change in pH, temp, and presence of 2-3 DPG

40
Q

In an oxygen dissociation curve, what is the normal Po2 (mm Hg), or O2 concentration in the environment

A

27 mm Hg

41
Q

In an oxygen dissociation curve what is the normal % O2 saturation

A

50%

42
Q

In an oxygen dissociation curve what is the normal P value

A

P50

43
Q

In an oxygen dissociation curve what will a shift to the left look like

A

P50 < 27 mm Hg
Higher oxygens affinity

44
Q

In an oxygen dissociation curve what will a shift to the right look like

A

P50 > 27 mm Hg
Lower oxygen affinity

45
Q

In an oxygen dissociation curve, what will cause a left shift (include Bohr effect)

A

Decreased body temp
Decreased 2-3 DPG
Decreased [H+]
Bohr effect:
Decreased H+ ions
Increased pH
Increased O2 affinity

46
Q

In an oxygen dissociation curve, what will cause a right shift (include Bohr effect)

A

Increased body temp
Increased 2-3 DPG
Increased [H+]
Bohr effect:
Increased H+ ions
Decreased pH
Decreased O2 affinity

47
Q

What are additional causes for a right or left shift

A

Altitude
Hypoxia (low O2 concentration)
Abnormal Hgb

48
Q

What is myoglobin

A

Resivoir for O2
High affinity for O2
Helps O2 when exercising

49
Q

What happens when CO2 levels increase in blood

A

Blood will become more acidic

50
Q

Hemoglobins oxygen binding affinity is

A

Inversely related both to acidity and to the concentration of CO2

51
Q

Describe the chloride shift

A
52
Q

Chloride concentration is lower in

A

Systemic venous blood than in systemic arterial blood

53
Q

In order to go through a membrane hemoglobin must be

A

Ferrous
Fe^2+

54
Q

What is the purpose of ferric irons

A

Storage and transport

55
Q

Hemoglobin is ______
Methemoglobin is ______

A

Ferrous (Fe^2+)
Ferric (Fe^3+)

56
Q

Always carry iron in what state

A

Ferric

CLS 307 (21 decks)

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