Hemoglobin

Question 1

What is another term for erythrocyte?

Answer 1

Red blood cell

Question 2

What is erythropoeisis?

Answer 2

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

Question 3

What are pluripotent stem cells?

Answer 3

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

Question 4

What is the process of erythropoeisis?

Answer 4

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

Question 5

What happens to the intracellular material in a erythrocyte?

Answer 5

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

Question 6

What is necessary for the production of many erythrocytes?

Answer 6

A lot of DNA is needed, folic acid and iron

Question 7

What is needed with folic acid and why?

Answer 7

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

Question 8

True or false?

Erythocytes are created in waves every 120 days

Answer 8

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

Question 9

Why do cancer drugs contain anti folates?

Answer 9

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

Question 10

Why do cancer chemotherapy patients experience anemia?

Answer 10

Because they cant make the DNA necessary for this erythropoeisis

Question 11

When blood is centrifuged what do the layers contain?

Answer 11

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

Question 12

What is the cellular material in blood called?

Answer 12

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

Question 13

What is the difference between plasma and serum?

Answer 13

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

Question 14

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

Answer 14

Buffy coat - represents the leukocytes. Very thin layer

Question 15

How do red blood cells get their shape?

Answer 15

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

Question 16

What is lost during the aging of blood cells?

Answer 16

The ability to deform. They are then recognized and deleted

Question 17

What is in blood cells?

Answer 17

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

Question 18

Why are there no mitochondria in blood cells?

Answer 18

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

Question 19

What is anemia and what are indications of anemia

Answer 19

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

Question 20

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

Answer 20

Tetramer and four globin chains. Tetrameric structure is important

Question 21

How many different types of subunits does hemoglobin have?

Answer 21

Two. Alpha and beta

Question 22

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

Answer 22

Four heme groups and four irons

Question 23

Why is iron toxic?

Answer 23

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

Question 24

What is a free radical?

Answer 24

An electron that is unpaired

Question 25

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

Answer 25

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

Question 26

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

Answer 26

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

Question 27

How many helices are in a subunit of a hemoglobin?

Answer 27

8 alpha helicies

Question 28

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

Answer 28

E7 and F8

Question 29

Where is Heme located in a subunit of hemoglobin?

Answer 29

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

Question 30

What are two characteristics of Heme?

Answer 30

Flat and fat (hydrophobic)

Question 31

What is the name for the His located at E7?

Answer 31

Distal His

Question 32

What is the name for the His located at F8?

Answer 32

Proximal His

Question 33

Is F8 or E7 closer to the iron and chelates?

Answer 33

F8

Question 34

What is a chelate?

Answer 34

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

Question 35

What is iron held by?

Answer 35

An organic compound

Question 36

What is the 5th chelation point?

Answer 36

Proximal F8 His

Question 37

What does the 5th F8 chelation do to iron

Answer 37

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.

Question 38

What is the 6th Chelation

Answer 38

Oxygen

Question 39

What does the 6th chelation do?

Answer 39

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

Question 40

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

Answer 40

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

Question 41

What are the types of globin chains?

Answer 41

Alpha-like and beta-like chains

Question 42

What are the sub-types of globin chains?

Answer 42

Alpha-like: zeta and alpha | Beta-like: epsilon, gamma, delta, beta

Question 43

What is a leghemoglobin?

Answer 43

Plant protein - active area of research

Question 44

A fertilized egg has what types of globin chains?

Answer 44

Zeta and epsilon

Question 45

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

Answer 45

Alpha and gamma

Question 46

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

Answer 46

Alpha and beta

Question 47

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

Answer 47

Alpha2 and beta2 are normal | Alpha2 and Delta2 are evolutionarily new

Question 48

What chain does oxygen bind to first?

Answer 48

Beta chain

Question 49

What are the two dimers of a hemoglobin?

Answer 49

Alpha 1 beta 1 | Alpha 2 beta 2

Question 50

Sickle cells look sickle because of what issue?

Answer 50

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

Question 51

Why do red blood cells need to be deformable?

Answer 51

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

Question 52

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

Answer 52

Cell is too large and it rips

Question 53

How many mutations cause sickle cell?

Answer 53

1

Question 54

Where is the mutation that causes sickle cell?

Answer 54

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.

Question 55

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

Answer 55

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.

Question 56

What is the function of hemoglobin?

Answer 56

Transport oxygen

Question 57

What are the mechanism of O2 binding to hemoglobin?

Answer 57

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

Question 58

What will help athletes in performance?

Answer 58

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

Question 59

What is blood doping

Answer 59

Add red blood cells in blood to increase compacity of vO2

Question 60

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

Answer 60

Iron Fe 2+.

Question 61

What is meth hemoglobin

Answer 61

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

Question 62

When meth hemoglobin forms what enzyme fixes it?

Answer 62

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

Question 63

What is cooperativity?

Answer 63

Biochemistry concept in which subunits interact with on another

Question 64

What is allosteric control

Answer 64

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

Question 65

What is the R state and T state of hemoglobin?

Answer 65

R-oxygenated | T-deoxygenated

Question 66

Myoglobin does what to oxygen?

Answer 66

Remove it from hemoglobin

Question 67

What is the structure of myoglobin?

Answer 67

Monomer that has one globin chain and one heme iron

Question 68

What has a higher affinity for oxygen. Myoglobin or hemoglobin

Answer 68

Myoglobin

Question 69

True or False: | The genes that form the alpha and beta subunits of hemoglobin are homologous?

Answer 69

True