hemoglobin

hemaglobin

a protien found in RBC’s

= heme molecule (contains iron) + globular proteins

what does a hemaglobin consist of

4 subunits

-4 globulin protiens

• each has 1 heme molecule

  • each has one iron with o2 bound

how many hemoglobins can each RBC hold

270 hb

each RBC can carry over a billion o2 molecueles

what does total O2 content of blood depend on

P_O2 and HB concentration

P_O2

directly propagational to amount of o2 available

(measure of the amount of o2 available)

what structure does a hemoglobin have

tertiary

forms of hemoglobins 

oxyhemoglobin, carbaminohemoglobin, carboxyhemoglobin

oxyhemoglobin

HB bound to O2 with varying affinity strength 

deoxyhemoglobin

Hemoglobin not bound to oxygen because it gave it to tissue for aerobic cellular respiration 

-now in a low affinity state 

carbaminohemoglobin

hemoglobin that is bound to co2

carboxyhemoglobin

hemoglobin bound to carbon monoxide

what does hemoglobin have the strongest bond with

CO than with o2 

-co is more preferred by the hemaglobin

percent HB-O2 saturation

% of oxyhemoglobin to total hemaglobin

why is percent HB-O2 saturation measured

to asses how well lungs have oxygenate the blood

-how may sub units have an o2 bound

(measure of gas exchange)

average percent HB-O2 saturation

97%

how is percent HB-O2 saturation measured

a pulse oximeter or blood-gas machine

loading of o2

when HB binds to o2 at the lungs

unloading of o2

when HB-O2 releases an o2 at the tissues

muscle contraction =

MLCK- dephos

MLC-phos

M.P-dephos

RHO Kinase-Phos

muscle relaxation

MLCK- phos

MLC-dephos

M.P-phos

RHO Kinase-dephos