Hemoglobin Model

Hemoglobin poseur note the 02 being carried by molecule. scream cleaners=subunits Green fen gamey=iron molecule Yel meek marsh mel humbled= oxygen molecule orangeness cards= heme groups (wolfe, 2000)Oxygenated/deoxygenated oxygenated 02 dancing buttonlike inflammation Subunit is in relaxed grad Higher 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 tense resile which has lower affinity for oxygen. When 02 binds todeoxygenated haemoglobin,hemoglobin transitions from Tstate to R state. This occurswhen 02 binds to iron, itcauses a multifariousness 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 stable in the T state which decreases its affinity for 02. Oxygen needfull y 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 high 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 reaping hook forms of hemoglobin.Normal and sickle red blood cells 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 bloodvessels. Blocks normal hemoglobinto deliver 02 to tissues. Short life hybridize of 10-20 days Body can not keep up with rbc product leading toanemia and pain. (Wolfe,2000)Normal Round nimbus shape Life span of long hundred days (Wolfe, 2000)(Ahern and Rajagopal, 2013)