lecture 7- hemoglobin/myoglobin

Question 1

40-50 % percent of blood volume is made of what

Answer 1

red blood cells = hematocrit

Question 2

what is the partial pressure of oxygen in the atmoshphere?

Answer 2

160 mmhg

Question 3

where is myoglobin found?

Answer 3

in the cytosol of the muscle

Question 4

doping ( erthyopoietin, transfusions, high altitude) all have danger in what? and why?

Answer 4

stroke..increases the visocity of the blood, make it hard to get through capillaries

Question 5

myoglobin stores for delivery to where?

Answer 5

mitochondria and metabolism

Question 6

what two other things are transported by hemoglobin?

Answer 6

NO and CO2

Question 7

what does NO do?

Answer 7

relaxation of muscle

Question 8

explain structures of, and percent of similarities,

Answer 8

proteins look very similar, however have different amino acid seqeucnes. only have leas than 25% amino acid homology

Question 9

which letters represent the alpha helical regions? in myoglobin

Answer 9

A-H

Question 10

70% of alpha helices are in what form?

Answer 10

rod like

Question 11

rod like characteristic of alpha does what?

Answer 11

provides stability, and hold on to prosthetic group

Question 12

N terminal starts with what letter?

Answer 12

A

Question 13

which amino acid aid in binding oxygen? and what are their names?

Answer 13

histidine . E7, F8

Question 14

what provides reserve supply of oxygen?

Answer 14

myoglobin

Question 15

how many major helical segments in myoglobin?

Answer 15

eight

Question 16

four of the helices are terminated by thwat residues?

Answer 16

proline

Question 17

what are the charged proteins in myoglobin

Answer 17

histidine

Question 18

what is the prosthetic portion?

Answer 18

ferroprotoporphyrin heme group

Question 19

what stabalizes the iron bond to molecular oxygen?

Answer 19

resonacne delocalization of the electron in the porphyrin ring

Question 20

oxygen does what to the ferrous group?

Answer 20

oxidizes it into ferric

Question 21

hemoglobin becomes what when ferrous becomes ferric?

Answer 21

methemoglobin

Question 22

which histidine dontates bond to oxygen?

Answer 22

E7, distal histideine

Question 23

ferrous group is coordinated to hoe many ligands or binding groups?

Answer 23

6

Question 24

oxygen binding curve for myoglobin is what shape?

Answer 24

hyperbolic

Question 25

what is the oxygen concentration in the capillaries?

Answer 25

20-30 mmhg

Question 26

myoglobin adjacent to capillaries is nearly what?

Answer 26

saturated

Question 27

what is the particlal pressure of oxygen at 50% saturation of the myoglobin?

Answer 27

2 mmhg

Question 28

what is the principal hemoglobin in adults?

Answer 28

hemoglobinm A1

Question 29

hemo globin is what type of graph? and what is it due to?

Answer 29

cooperativity sigmoidal

Question 30

when oxygenated hemoglobin moves to tissues wihth partial pressure of 20 mmhg the saturation level of hemoglibin drops to what? what percent of potential oxygen binding sites contribute?

Answer 30

32% 66%

Question 31

the binding of the first oxygen molecule to each hemoglobin molecile enhances the binding of the second oxygen molecule by a facor of what?

Answer 31

3

Question 32

when 3 oxygens are bonded to a hemoglobin, what is the affinity for the fourth oxygen molecule?

Answer 32

20 times that of full deoxy

Question 33

the strongest contacts are between which two things?

Answer 33

alpha and beta

Question 34

how far does iron move upon oxygenation?

Answer 34

.4

Question 35

on oxygenation, what is the rotation between alpha one and beta one?

Answer 35

15 degrees

Question 36

BPG stabailizes what?

Answer 36

the deoxy form of hemoglobin

Question 37

hydrogen atoms, and carbon dioxide all favor what?

Answer 37

the deoxy form

Question 38

histidine beta 143 is replaces by what in fetal hemoglobin?

Answer 38

serine

Question 39

who do fetal hemoglobin have a higher affinity for oxygen than maternal?

Answer 39

the replacing of histidine with serine, decreases affinity for BPG, and therefor binds oxygen more readily

Question 40

what is the prinicipal hemoglobin in fetal? consisting of which chains?

Answer 40

hemoglobin F. 2 alpha and 2 gamma

Question 41

as you increase the PH, what happens to oxygen affinity?

Answer 41

as decrease PH, you decrease oxygen affinity

Question 42

what is the haldane effect?

Answer 42

deoxygenation of the blood increases its ability to carry carbon dioxide

Question 43

how does a oximeter measure pulse?

Answer 43

measuring absorption of hemoglobin and myoglobin. they absorb diff wave lengths

Question 44

is full oxygenated hemoglobin diamagnetic or para? magnetic or non

Answer 44

dia. non

Question 45

is deoxy diamagnetic or para? magnetic or not?

Answer 45

para. magnetic

Question 46

how does magnetic resonance imaging work?

Answer 46

measures amount of diamagtnetic and paramagentic in brain to see which part is working.

Question 47

sickle cell anemia causes what as far as dental work

Answer 47

block capillaries and rupture, inflammation, pain, poor bone development, gingival lesions, caries, perio, anema, infections, renal failure

Question 48

sickle cell is caused by what?

Answer 48

a change from glutamate to a valine in position 6 on the neta 1 strand

Question 49

what do sickle cells tend to do in blood?

Answer 49

aggregate together forming long fibers, causing hydrophobic interactions

Question 50

does sickle cell have a higher or lowe PI than normal hemoglobin?

Answer 50

higher

Question 51

what is thalassemia cause by?

Answer 51

caused by loss of single hemoglobin chain, leading to low levels of functional hemoglobin, and decreased production of red blood cells leading to anema

Question 52

alpha thalessemia causes loss of what?

Answer 52

cooperativity