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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
Name the 4 intrauterine Hgbs
Gower - 1 Gower - 2 Portland Hgb F
26
What makes up Portland Hgb and when is it present
2 Xi 2 gamma 1st 8 weeks of intrauterine life
27
What makes up Gower 1 Hgb
2 Xi 2 epsilon
28
What makes up Gower 2 Hgb
2 alpha 2 epsilon
29
What makes up the abnormal Hgb H and why
4 beta It will bind to itself if there is not enough alpha
30
What makes up the abnormal Hgb Bart’s and what is the result
4 gamma If there is no alpha at all, the child will not survive
31
What is Hgb A1c and what percent of it is found in adult Hgb
Glycohemoglobin Hgb with glucose attached/binded 4-6%
32
If glycohemoglobin is lower than normal, what does that tell you
Something is wrong with the longevity of RBCs where they are being destroyed too early (anemia)
33
What can Hgb A1c tell us?
Diabetes Gives us an idea about the patient's diet With an increase in glucose in blood, it will be present in urine
34
How does CO2 travel from tissue to lungs
CO2 combines with water and becomes an ion to transport. Once it reaches the lungs it dissociates and reverts back to CO2
35
What percent of CO2 can dissolve
20-30%
36
What is the normal pH
7.35-7.45
37
What pH is wanted in your tissues
7.35
38
How does O2 get released from Hgb
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
On an oxygen dissociation curve, how do you push the graph to facilitate Hgb to let go of O2
Change in pH, temp, and presence of 2-3 DPG
40
In an oxygen dissociation curve, what is the normal Po2 (mm Hg), or O2 concentration in the environment
27 mm Hg
41
In an oxygen dissociation curve what is the normal % O2 saturation
50%
42
In an oxygen dissociation curve what is the normal P value
P50
43
In an oxygen dissociation curve what will a shift to the left look like
P50 < 27 mm Hg Higher oxygens affinity
44
In an oxygen dissociation curve what will a shift to the right look like
P50 > 27 mm Hg Lower oxygen affinity
45
In an oxygen dissociation curve, what will cause a left shift (include Bohr effect)
Decreased body temp Decreased 2-3 DPG Decreased [H+] Bohr effect: Decreased H+ ions Increased pH Increased O2 affinity
46
In an oxygen dissociation curve, what will cause a right shift (include Bohr effect)
Increased body temp Increased 2-3 DPG Increased [H+] Bohr effect: Increased H+ ions Decreased pH Decreased O2 affinity
47
What are additional causes for a right or left shift
Altitude Hypoxia (low O2 concentration) Abnormal Hgb
48
What is myoglobin
Resivoir for O2 High affinity for O2 Helps O2 when exercising
49
What happens when CO2 levels increase in blood
Blood will become more acidic
50
Hemoglobins oxygen binding affinity is
Inversely related both to acidity and to the concentration of CO2
51
Describe the chloride shift
52
Chloride concentration is lower in
Systemic venous blood than in systemic arterial blood
53
In order to go through a membrane hemoglobin must be
Ferrous Fe^2+
54
What is the purpose of ferric irons
Storage and transport
55
Hemoglobin is ______ Methemoglobin is ______
Ferrous (Fe^2+) Ferric (Fe^3+)
56
Always carry iron in what state
Ferric

CLS 307 (21 decks)

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