bisc208 gas exchange

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11 Terms

1
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hemoglobin

-protein tetramer made of four subunits

-main component of RBCs

2
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composition of hemoglobin

4 polypeptide chain subunits

-2 alpha, 2 beta

3
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subunits of hemoglobin

contains a heme group

-a porphyrin ring with a Fe at the center that binds O2

4
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O2 saturation of Hb graph

-y-axis: Hb saturation (%), average # of O2 molecules bound to Hb

-x-axis: pO2

5
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% saturation of Hb

(amount of O2 bound/max amount that could be bound) x 100

6
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O2 binding to Hb is cooperative, what does this mean?

-binding of each O2 causes a conformational change making it progressively easier for more O2 to bind

-once pO2 drops —> Hb is more likely to release O2 (reverse)

7
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what is the relationship between pO2 and Hb saturation?

-s-shaped, nonlinear

-at 60 mmHg, O2 is 90% saturated

8
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O2-Hb binding

-O2 released from Hb while traveling through capillaries

-oxygen reserve

-exercise produces a significant drop in pO2

9
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O2 saturation at rest

75% (sea level)

10
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O2 saturation as it leaves lungs

98% (sea level)

11
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oxygen reserve

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