L8 Flashcards

1
Q

What 2 proteins are responsible for O2 storage and transport?

A

hemoglobin and myoglobin

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2
Q

what is hemoglobin?

A

hemoglobin is the red blood pigment exclusively present in erythrocytes(RBC)

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3
Q

List all 4 types of hemoglobin that are synthesized in the human body throughout its life span and explain when they are present . .

A

Hbε(epsilon) :Present in embryonic life ( Hb Gower-1). Composed of 2 - ζ(zeta) and 2 - ε chains.

HbF:Fetal stage (Second trimester till birth). Composed of 2 – α and 2 – γ chains.

Hb A1:Major normal adult Hb (Starts with birth and reaches completion by around 6 months). Composed of 2 - α and 2 - β chains.(gamma gene is almost off)

Hb A2:Minor normal adult Hb Composed of 2 - α and 2 - δ (delta) chains.

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4
Q

what is the normal adult blood content?

A

Hb A1 - 97%
Hb A2 - 2%
Hb F - 1%

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5
Q

what is the function of hemoglobin of hemoglobin and myoglobin ?

A

hemoglobin transports blood

helps with transport co2 from tissues to lungs

acts as buffer

while myoglobin stores it . if there is not enough hemoglobin then hemoglobin anemia will occur

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6
Q

how many oxygens can hemoglobin and myoglobin bind too , how many chains do they have ?

A

hemoglobin can hold 4 oxygens while myoglobin can only hold 1

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7
Q

all hemoglobin are hetro-tetramere

A

.

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8
Q

describe the structure of hemoglobin A1

A

IT IS A CONJUGATED PROTEIN . HEME BEING THE PROSTHETIC GROUP

 Globin (96% of Hb)

4 polypeptide chains of two different primary structures (2 - α and 2 - β chains)
Each chain has one heme group attached to it.

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9
Q

What is the heme inside the ?

A

complex of iron Fe++ ferrous and protoporphyin (has 4 pyrrole rings )

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10
Q

what are the 6 bonds Fe++ forms ?

A

4 with the N of porphyrin.
On one side of the plane with a.a histidine (proximal) of the globin.
The other side with O2.
1 Hb can bind and transport 4 O2

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11
Q

describe the structure of a myoglobin.

A

conjugated protein with prosthetuic group being skeletal muscles and cardiac muscles

consists of one pollypeptide chain (monomeric)

has 1 molecule of heme attached

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12
Q

In the muscles:
Mb acts as an O2 storage protein in muscles.
O2 is taken up and stored by Mb.
Mb has high affinity for O2 than Hb.

A

.

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13
Q

the ODC for myoglobin is?

A

hyperbolic . it shows high affinity for oxygen (uptight)

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14
Q

the ODC for hemoglobin is ?

A

sigmoidal. has comparatively low affinity for oxygen. this also indicates that binding of O2 to Hb is cooperstive . binding of O2 to one heme increases binding affinity of O2 to other hemes of the same Hb molecule

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15
Q

there is communication among subunits in the hemoglobin function

A

..

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16
Q

what major forms are co2 present in the body.

A

Dissolved CO2
Bicarbonate (HCO3-)
Carbaminohemoglobin (Carbon dioxide linked to hemoglobin)

17
Q

explain co-operative bining.

A

binding of O2 to one heme increases binding affinity of O2 to other gmes of the same Hb molecule . thgis occurs because there is communication among subunits in the hemoglobin function