Bohr Effect - Educational Materials

Boher effect "Albsteric effectors Or uptake Lungs, R. form + O2 offinity ↑PO₂ theme-heme interaction ↑PH & makes ionic bond wek -PCO2 weak ionic bonds. Negative affectar O2 release Tissue T-Form Or offinity Poz PH 1. Pror] strong lone bond 2.3BPG T-Porm *CO₂ transporte - 70-80% is transported as Bicarbonate CO2 + H2O H2CO3 Zinc Carbonic anhydrase HHCO3 20-25% is transported as Carbamate Carbamino" CO2 binds B-subunit with ami-p group and. Support J-form for Oz release CO2 CO2 Positive allostenics -PH -Acidic PH at tissue levels 1 ionization of imidazole ring shat found in B-s urut -acidic PH support J-form and 1 O2 release totisswe acidic PH make salt bridge stronger: J. Porm low PH H -2,3 BPG2,3 Bis Phospho glycerate » Glucose Glycolysis 2,3 BPG Coo P make T-form P for Oz velease RBC Q -2,3BPG does not offect (HbF).. & subunit... -2,3 BPG is highly negative, bind to apocket between B-suburit of HbA, and support J-form for Oz release R-form B 20 T-frum B1 Jonsine is Converted to 2,3 BPG; Inosine is added for blood storage in banks to maintain 2,3BPG levels 2,3BPG blood stor Inosine Hypoxanthine ring ribose High attitude, smoking, anemia, emphysema Hypoxia 2,3 BPG" Faster Oz velease CO Poisoning Carbon monoxide... Co binds 200 times to heme faster Than Oz Co support R-form and Or affinity to the other subunits 11 Oz release 11 CO + Hb = Carboxy hemoglobin -Treated by [hyperbaric Oz 100%] Oz hemoglobin disseciation Curve & 1 mmHg of Po₂ to 50% saturate myoglobin 26mmHg of Po₂ to 50% saturate tremoglobin - -100 mmHg of PO2 to 97% saturate both - @myoglobin has more Oz offinity than hemoglobin sakiration 100 more Oz affinity G "Hyperbolic Curven myoglobin Tertiary) Hemoglobin Q Quaternary hess Or affinity Sigmoidal Curve) So 10 20 10 50 Pot mity) - Notes -myoglobin produce hyperbolic Curve - hemoglobin produce sigmoidal Curve _CO2, low PH, 2,3 BPG 102 arthinity of hemoglobin (shifting sigmoidal Curve to right, Q * bohr shift POz, high PH, CO 10r afhinity of hemoglobin u shifting sigmoidal curve to loft bohr shift. *Hemoglobino Pathies Genetic defectAutosomal recessive Causes abnormal Hb synthesis short RBC life span 10-14 day Hemolytic anemia Disease mutation or Trai't M Sickle cell anemia Homozygote X defect Disease Hetrozygote XTrait or carrier z more in africans -anemia, Pallor, jaundice Rod of hemoglobin distort RBC shape specially at tissue level (↑CO2, PH, 2,3 BPG -life span lo-14 day (resistance to malaria water insoluble HbS "protein separation, move slower than HbAi at electrophoresis -mutation of B-chain at position 6 the normal glutamate is replaced by water insoluble valine 1469.9 instead of glutamate 196a-a valin 123456 Fe sticky spot "B-chain" slow fast +ve lyst val HbS glu electrophoresis >> Alkaline PH * Treatment 8- -Repeated blood transfusion that may Cause iron overload Hemosiderosis Iron overload can be treated by (injection of Desferroxamine Sickle cell anemia Homozygote > sever anemia short RBC life span DDD - Elevated HbF even after 6 months Hemoglobin C diseases- mild hemolytic anemia mutation of B-chain Cys sickle cell trait... Heterozygote _mild anemia normal RBC are found - 888 _ not elevated - *Hemoglobin SC disease &- rare anemia, mixed, HbS, HbC Thalassemia -Decrease or absent subunit synthesis la or B - -Thalassemia vor absent. x- subunit BO By Abnormal Hb Hb Barts -mutation of 4 genes in Chromosome 16 -Defect of only one gene silent camier >> -Defect of two geries 11 - Thalassemia trait> -Dofect of 3 genes & Chalassemia disease HbH -Dofect of 4 genes sever disease leads to Hydropes Petali's •B-Thalassemiator absent B-chain synthesis ↑ HbF even ofter 6 months Fetal Hb -Treated by repeated blood transfusion. B-Thalassemia major Cooley's anemia Trait B-Thalassemia minor. Homozygote Heterozygote. - sever anemia (short lifespor - mild anemia -↑ HbF Require blood Trans Fusion" - HbF is normal * physical properties of a.a 1-Solubility - a.a are water soluble Insoluble in organic solvents Cystine, Tyrosine are poorly water soluble. Proline, hydroxyproline are soluble in alcohol. 2.Ultraviolet absorbtion Aromatic aas absorb ultraviolte phe Tvp His Tyrosine at 280 nm *Chemical properties of a.a. 1- Reactions with Ninhydrin produce blue color with most aias except proline, hydroxyproline produce yellow color 2-Reaction with floure scaminen blue color si Same as Ninhydrin but it's more sensitive to detect nanograms of as 3- Chelation (Amino acid + metals) 2 Glycine acidic base Ca +2 Chelation Calcium diglycinate Salt excreted in urine Biologically active peptides (primary proteins Glutathione 2. vasopressin Oxytocin N (Vasoconstriction) (milk ejection) nonapeptide ↑ blood pressure uterine Contraction). 3. In myosin of skeletal muscles there are dipeptides -Carnosine B-alany/ histidine >> Anserine B-alanyl methyl histidine >> • non standard aas Histidine decarboxylase Histamine Allergy" Vit. Bo Anaphylaxis CO2 -Tyrosine decarboxylase DOPA Dopamine vit.BG Norepinephrine Epinephrine Catecholamines I I -Tyrosine Jo. 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