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- 626: Regarding thioamides: ale lon (a) they include chlorambucil (b) methimazole is less potent than propylthiouracil (c) the bioavailability of propylthiouracil is less than 25% (d) their prolonged use may result in gastrointestinal distress (e) the most dangerous complication is agranulocytosis4 A I. Refer to the figure below and answer the following questions: 45 5 55 6 65 PH 7 75 8.5 0 10 B 15 20 25 30 35 Temperature (°C) 40 45 Legend: Blue - wild-type ß-galactosidase; Red - mutant ß-galactosidase a. What is the optimum pH of wild type ß-galactosidase? b. What is the optimum temperature of mutant ß-galactosidase? c. Which enzyme has the greater activity at pH 7.2? d. Which enzyme has the greater activity at a temperature of 42.5°C? e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C? 50 55
- 8) what as the reasons for me asuning a colored compound the absoobance of at 9ts À max9 the range of visible light a) A max b) Absoobance is moe accurate, Hhe determing sensitivity to distinguis h too in will be loweyt enor conco C) Better diff. conemical Compounds Better sensitiw'ty to distingueyb teoo d) Sturil ar conc. off Same chemical compoud.125. A 27-year-old woman who is at 17 weeks' gestation has an increased serum concentration of a-fetoprotein. Ultrasonography should be performed to investigate for which of the following abnormalities in the fetus? A) Agenesis of the corpus callosum B) Anencephaly C) Congenital hydrocephalus OD) Holoprosencephaly E) Micrencephaly3. The image below depicts 2,3-bisphosphoglycerate depicted in dark gray, and ß subunits are depicted in light gray. (BPG) bound to hemoglobin. The a subunits are BPG (a) Briefly explain how BPG regulates oxygen transport by hemoglobin and describe the critical chemical properties of BPG and its binding pocket.
- Number 3. I would say no burn can’t explain why’s exactly. IS it right? And how would I explain why?2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His…111. Which of the following best describes the relative quantities of the subunits of hemoglobin in a healthy full-term newborn at birth? OA) a> ß>y> 5 O B) a>y> ß > d C) B >x>5 > y Y OD) B > Y D) B OE) y > ß>5 > α >y>a> d
- 5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION8. In a patient with anemia, the presence of Heinz bodics in the RBCS was the result of the hemoglobin subunits aggregation due to the oxidation of -SH groups of Hb cysteine residues with active oxygen forms and the formation of disulfide bonds. What metabolic disorders in the RBC can be the cause of this clinical case? To solve the problem: a) indicate which reactions maintain cysteine residues in a reduced state; b) name the coenzyme involved in this process, write a diagram of the process in which the reduced form of this coenzyme is formed; c) indicate the enzyme which deficiency may lcad to a lack of the reduced cocnzyme and be the cause of the clinical case described above.`Expand the term VNTR?