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Biochemistry-Jourdan > Hemoglobin > Flashcards

Hemoglobin Flashcards

1
Q

What is another term for erythrocyte?

A

Red blood cell

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2
Q

What is erythropoeisis?

A

From pluripotent stem cells erythrocites are produced. This starts in the bone marrow

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3
Q

What are pluripotent stem cells?

A

Cells that are completely undifferentiated and depend on extracellular signals to dictate what it is going to become

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4
Q

What is the process of erythropoeisis?

A

A single cell is going to divide and then a signal is given and then it divides again. From one cell 2^11 mature erythrocytes are formed

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5
Q

What happens to the intracellular material in a erythrocyte?

A

It is ejected out and is becomes just a bag of hemoglobin

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6
Q

What is necessary for the production of many erythrocytes?

A

A lot of DNA is needed, folic acid and iron

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7
Q

What is needed with folic acid and why?

A

B12 because folic acid can mask the symptoms of deficiency of B12

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8
Q

True or false?

Erythocytes are created in waves every 120 days

A

False. A steady stream of new blood is needed. Constantly producing and constantly deleting blood cells

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9
Q

Why do cancer drugs contain anti folates?

A

Messes with the folic acid system and cant make DNA and therefore kill the cancer

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10
Q

Why do cancer chemotherapy patients experience anemia?

A

Because they cant make the DNA necessary for this erythropoeisis

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11
Q

When blood is centrifuged what do the layers contain?

A

Cellular material goes to the bottom and non cellular goes to the top

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12
Q

What is the cellular material in blood called?

A

Hermatocrite and is about 50% of the blood. Packed with blood

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13
Q

What is the difference between plasma and serum?

A

Plasma: Has an anti coagulate added to the blood and becomes the layer at top when centrifuged
Serum: Blood coagulates first then spun; becomes the top as well

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14
Q

Once the noncellular portion is removed from blood and spun in centrifuge what is the top layer called?

A

Buffy coat - represents the leukocytes. Very thin layer

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15
Q

How do red blood cells get their shape?

A

A specialized cytoskeleton system that laminates the innermembrane. Attaches to the inner membrane and actively deform through microcirculation (test tube capillaries)

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16
Q

What is lost during the aging of blood cells?

A

The ability to deform. They are then recognized and deleted

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17
Q

What is in blood cells?

A

Hemoglobin at 37% solution. ATP Source, Pentophosphate pathway, other upport pathways but no organelles.

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18
Q

Why are there no mitochondria in blood cells?

A

Because it would steal the O2 and it would be a conflict of interest

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19
Q

What is anemia and what are indications of anemia

A

Low red blood cell count is anemia. Indications are low hermatocrite and hemoglobin. Other tests include paleness of blood which indicates low iron

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20
Q

What type of Quaternary structure does hemoglobin have and how many chains?

A

Tetramer and four globin chains. Tetrameric structure is important

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21
Q

How many different types of subunits does hemoglobin have?

A

Two. Alpha and beta

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22
Q

For every terameric structure how many heme groups and irons are in hemoglobin?

A

Four heme groups and four irons

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23
Q

Why is iron toxic?

A

If in the blood it will catalytically produce free radicals. Iron can go back and forth between 2+ and 3+. Can spontaneously react with proteins and DNA

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24
Q

What is a free radical?

A

An electron that is unpaired

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25
Q

What is “crashing” of a red blood cell and what can cause it?

A

Crash is the release of intracellular materials from red blood cells and can be caused in severe situations especially rigorous exercise like marathons

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26
Q

What are the 3 plasma proteins that grab released intracellular material of a crashed red blood cell?

A

Heptaglobin - grabs hemoglobin
Hemopexin - grabs heme
Transferin - Grabs iron

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27
Q

How many helices are in a subunit of a hemoglobin?

A

8 alpha helicies

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28
Q

Which two His participate in the control of oxygen bonding to the iron and the heme?

A

E7 and F8

29
Q

Where is Heme located in a subunit of hemoglobin?

A

Between the E,F and G helices in a hydrophobic pocket

30
Q

What are two characteristics of Heme?

A

Flat and fat (hydrophobic)

31
Q

What is the name for the His located at E7?

A

Distal His

32
Q

What is the name for the His located at F8?

A

Proximal His

33
Q

Is F8 or E7 closer to the iron and chelates?

A

F8

34
Q

What is a chelate?

A

a compound containing a ligand (typically organic) bonded to a central metal atom at two or more points

35
Q

What is iron held by?

A

An organic compound

36
Q

What is the 5th chelation point?

A

Proximal F8 His

37
Q

What does the 5th F8 chelation do to iron

A

Pulls the iron out of the plane. There are four other chelation points around the hem and form a plane and iron is stuck symmetrically in the plane.

38
Q

What is the 6th Chelation

A

Oxygen

39
Q

What does the 6th chelation do?

A

Oxygen the 6th chelation, will come in on the other side and bind to iron and click it into place.

40
Q

When the 6th chelation is added what happens to the molecule as a whole?

A

Iron clicking into place initiates a cascade that the whole molecule clicks into a different shape

41
Q

What are the types of globin chains?

A

Alpha-like and beta-like chains

42
Q

What are the sub-types of globin chains?

A

Alpha-like: zeta and alpha

Beta-like: epsilon, gamma, delta, beta

43
Q

What is a leghemoglobin?

A

Plant protein - active area of research

44
Q

A fertilized egg has what types of globin chains?

A

Zeta and epsilon

45
Q

At the stage of a fetal what types of globin chains are in hemoglobin?

A

Alpha and gamma

46
Q

By the age of one year what types of globin chains are in hemoglobin?

A

Alpha and beta

47
Q

What is the normal globin chains found in adults? What is the new combinations recently developed (20 million years)

A

Alpha2 and beta2 are normal

Alpha2 and Delta2 are evolutionarily new

48
Q

What chain does oxygen bind to first?

A

Beta chain

49
Q

What are the two dimers of a hemoglobin?

A

Alpha 1 beta 1

Alpha 2 beta 2

50
Q

Sickle cells look sickle because of what issue?

A

14 hemoglobin molecules bundle up and want to rip out. Growing pole vault polymerizing and starts to bend against the sides of the cell.

51
Q

Why do red blood cells need to be deformable?

A

In order to pass through the micro capillary bed and wiggle through. The blood vessels have a narrower diameter than red blood cells.

52
Q

What happens when a sickle cells passes through narrow blood capillary beds

A

Cell is too large and it rips

53
Q

How many mutations cause sickle cell?

A

1

54
Q

Where is the mutation that causes sickle cell?

A

On the a helix on the with amino acid (A6). The beta chain. Normally it is a glutamate but it goes to a valine in sickle cell. Nonconservative substitution.

55
Q

Why can’t the A6 amino acid be a valine instead of glutamate?

A

Glutamate is acidic and hydrophillic and valine is branched and hydrophobic. Nonconservative. There is a hydrophobic patch on the outside. And that patch becomes more extreme in the deoxygenated state.

56
Q

What is the function of hemoglobin?

A

Transport oxygen

57
Q

What are the mechanism of O2 binding to hemoglobin?

A

Fe 2+ : O2 binding sites
Cooperativity
Reversible binding
Also steric control

58
Q

What will help athletes in performance?

A

Veomax. Maximum volume of oxygen one can consume. How much oxygen you can get to muscles

59
Q

What is blood doping

A

Add red blood cells in blood to increase compacity of vO2

60
Q

Oxygen binds to what molecule in hemoglobin and it what oxidative state?

A

Iron Fe 2+.

61
Q

What is meth hemoglobin

A

When Fe is in 3+ state. Oxidized state. Can bind to hemoglobin but can’t be relinquish

62
Q

When meth hemoglobin forms what enzyme fixes it?

A

Meth hemoglobin reductase which requires Cytochrome B5 and NADH to supply the electrons.

63
Q

What is cooperativity?

A

Biochemistry concept in which subunits interact with on another

64
Q

What is allosteric control

A

Compounds that do not bind to the active sites. Bind elsewhere to change the conformations. H+ and CO2 force hemoglobin to the T state.

65
Q

What is the R state and T state of hemoglobin?

A

R-oxygenated

T-deoxygenated

66
Q

Myoglobin does what to oxygen?

A

Remove it from hemoglobin

67
Q

What is the structure of myoglobin?

A

Monomer that has one globin chain and one heme iron

68
Q

What has a higher affinity for oxygen. Myoglobin or hemoglobin

A

Myoglobin

69
Q

True or False:

The genes that form the alpha and beta subunits of hemoglobin are homologous?

A

True

Biochemistry-Jourdan (8 decks)

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