Identify the species that are liganded to the porphyrin ring Fe(II) ion in deoxyhemoglobin (i.e., Hb in the T state). H₂O Oxygen Nitrogen atoms in the porphyrin ring His F8 (the proximal his) His E7 (the distal his)
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- A notable increase of the activities of CPK МВ (creatine phosphokinase? MB isoform) and LDH-1 were revealed at examination of patient’s blood. What is the most likely pathology?A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?Using the information given, determine the Kd for the binding of HABA to BSA. B= y-intercept (E bound) 2457.6x (E unbound) Data for the binding of HABA to BSA y = 4E-06x + 5.2134 R² = 0.928
- From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.Kindly mention the indications for clopidogrel in acute coronary syndrome (ACS). Should it be used along with aspirin or alone if the latter is contraindicated? Are there any studies that combine both with either low-molecular-weight heparin (LMWH) or unfractionated heparin? How long should clopidogrel be continued?What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.
- If normal plasma pH is 7.4 and normal [CO2) is 1.2 mM, what is the normal (HCO321? The pK9 for this system is 6.1. Phosphoric acid (H3PO4) has three dissociable protons, with the pK,'s shown below. Which form of phosphoric acid predominates in a solution at pH 4? Explain your answer. Acid H3POA 2.14 H2PO4 6.86 HPO,2- 12.4Why is salbutamol better than isoproterenol in asthma management in terms of their binding sites?Why valinomycin is highly selective for K+ relative to Na+? (Subject: Biomembrane)
- Explain why the proteins involved in blood clotting, fi brin and thrombin, are fi rst synthesized as the zymogens fi brinogen and prothrombin, respectively.A series of novel phenadoxone derivatives without mu2 receptor activity (mu2 activity is responsible for physical dependence) proposed to be developed as analgesics is shown below. Addition of which heterocyclic substituent R to phenadoxone is LIKELY to cause the MOST binding of the corresponding derivative to plasma proteins? Use the additivity of approximate estimates of logP to answer this question. phenadoxone derivatives A. Azetidine B. Thiophene C. Oxetane D. Furan E. Pyrrole ترف لي تي في R= -NHAllosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformation