hemoglobin Flashcards

1
Q

hemoglobin is an ___ protein

A

allosteric

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2
Q

95% of a red blood cell is ___

A

hemoglobin

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3
Q

T/F: animals lower than mammals still have a nucleus in their red blood cells

A

true

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4
Q

Heme is a type of ___ just like chlorophyll.

A

porphorin

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5
Q

visual/structural difference between oxy and deoxy hemoglobin

A

Deoxy : has a little white space in the middle of the tetramer
Oxy: no space. When its carrying oxygen, shape shifts, closes.

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6
Q

function of biphosphoglycerate? (BPG)

A

facilitates the release of o2; does so by stabilizing the T state, plugging itself into the hole in deoxyhemoglobin.

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7
Q

BPG acts as what kind of inhibitor

A

hetertropic (remember, homotropic would be same substance)

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8
Q

hemoglobin helps animals to be able to bind oxygen in the ___ and deliver it to the ___

A

lungs, tissues

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9
Q

where is partial pressure of oxygen highest

A

lungs

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10
Q

where can both myoglobin and hemoglobin pick up oxygen

A

lungs, due to high partial pressure

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11
Q

The oxygen affinity of fetal red blood cells

A

The oxygen affinity of fetal red blood cells is higher than that of maternal red blood cells because fetal hemoglobin does not bind 2,3-BPG as well as maternal hemoglobin does. Fetal hb consists of 2 alpha and 2 gamma chains. The gamma chains have lower affinity for 2,3-bisphosphoglycerate than the beta chains of maternal hb.
(recall that BPG facilitates RELEASE of O2)

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12
Q

how does CO2 promote the release oxygen

A

As CO2 dissolves in tissues, they become slightly more acidic than the lungs.
Low pH allows the formation of ionic interactions -> stabilize T state of hemoglobin -> facilitate oxygen release

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13
Q

is the pH drop the only reason that CO2 in lungs facilitates oxygen release?

A

no! Since both CO2 and H+ are inhibitors: both affect release of oxygen in the tissues.

Both pH and CO2 have separate effects on hemoglobin causing them to release more oxygen in the tissues. Now we can dump off 88% in tissues and pick up nearly 100% in the lungs.

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14
Q

how is sickle cell anemia caused?

A

A small mutation that caused a change in one of the hemoglobin chains such that valine was inserted where glutamate should have been. Ends up forming long fibrils instead of a sphere. Sickles the shape of the cell. Still carry oxygen but clog up the capillaries.

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15
Q

oxygen binds to hemoglobin ____

A

homotropically

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16
Q

what are Hb’s 3 mechanisms for releasing more O2?

A

Hb has three mechanisms which stabilize the T state to lower the affinity for oxygen in the tissues compared to the lungs. 2,3-bisphosphoglycerate, CO2, and H+ act as
heterotrophic inhibitors. These three regulators allow more oxygen to be released where it is needed

17
Q

describe the contents of a hemoglobin molecule

A

Hb is a tetramer with 2 alpha and 2 beta chains, each of which have a heme prosthetic group with Fe2+ to bind oxygen