Hemoglobin Model

Hemoglobin model note the 02 being carried by molecule. call cleaners=subunits Green marsh mellow=iron molecule discolour marsh mellow=oxygen molecule Orange cards= haem groups (wolfe, 2000)Oxygenated/deoxygenated oxygenated 02 rebound Bright red Subunit is in relaxed form racy affinity for 02 Affinity for oxygen iscooperative, which meansthat the affinity for 02increases with each boundmolecule. ( Ahern & Rajagopal, 2013)Deoxygenated 02 not bound Dark red color In filter form which has pooh-pooh affinity for oxygen. When 02 binds todeoxygenated hemoglobin,hemoglobin transitions from Tstate to R state. This occurswhen 02 binds to iron, itcauses a change in thesubunit. ( Ahern & Rajagopal,2013)Bohr Effect Hemoglobin has a high affinity for 02 at a high PH, low Co2. Hemoglobin has a lower affinity at a low PH, high Co2.At a high Co2, low PH hemoglobin is more unchangeable in the T state which decreases its affinity for 02. Oxygen needs to be delivered to the tissues. Tissues have a low PH. Hemoglobin needs to release 02 at low PH. Low PH = low 02 saturation.( Wolfe,2000 )Myoglobin wants to store 02 for when tissues need it. Has a higher affinity than hemoglobin. ( Ahern & Rajagopal, 2013) Hemoglobin wants to unload 02 in the tissues. Has a lower affinity than myoglobin. ( Ahern & Rajagopal, 2013 )(Genetic science learning center, 2013)Difference between normal and sickle forms of hemoglobin.Normal and sickle erythrocytes at the cellular level.(Genetic science learning center, 2013)Diseased RBCs vs. Normal RBCs Diseased Have a sickle shape, and arethick and sticky. Clumpstogether in small demarcationvessels. Blocks normal hemoglobinto deliver 02 to tissues. Short life span of 10-20 old age Body can not keep up with rbc output signal leading toanemia and pain. (Wolfe,2000)Normal Round Doughnut shape Life span of 120 days (Wolfe, 2000)(Ahern and Rajagopal, 2013)