Description : A shift in the oxygen-haemoglobin dissociation curve to the right occurs in : a. hypothermia b. carboxyhaemoglobin c. acidosis d. fetal haemoglobin
Last Answer : acidosis
Description : Given below graphs an oxygen dissociation curve `:-` Where in the body will haemoglobin be saturation at the percentage shown at points X,Y and Z.
Last Answer : Given below graphs an oxygen dissociation curve `:-` Where in the body will haemoglobin be ... ventricle , Y-Right ventricle, Z-Systemic artery
Description : The oxygen - haemoglobin dissociation curve will show a right shift in case of
Last Answer : The oxygen - haemoglobin dissociation curve will show a right shift in case of A. High `pCO_(2)` B. High ... `pCO_(2)` D. Less `H^(+)` concentration
Description : The oxygen Haemoglobin dissociation curve will show a right shift in case of `:-`
Last Answer : The oxygen Haemoglobin dissociation curve will show a right shift in case of `:-` A. Less `H^(+)` concentration B. ... `CO_(2)` D. High 2,3, D.P.G.
Description : Oxygen dissociation curve of haemoglobin is
Last Answer : Oxygen dissociation curve of haemoglobin is A. Hyperbolic B. Sigmoid C. Straight D. Constant
Description : Oxygen haemoglobin dissociation curve will shift to right on decrease of
Last Answer : Oxygen haemoglobin dissociation curve will shift to right on decrease of A. Acidity B. Carbon dioxide concentration C. Temperature D. pH
Description : Iron is stored in the form of (A) Ferritin and transferrin (B) Transferrin and haemosiderin (C) Haemoglobin and myoglobin (D) Ferritin and haemosiderin
Last Answer : Answer : D
Description : Carbon dioxide entering the red blood corpuscles from the tissues is partially taken up by haemoglobin to form (a) carboxyhaemoglobin (b) carbonylhaemoglobin (c) carbaminohaemoglobin (d) carbomoylhaemoglobin
Last Answer : Ans:(a)
Description : Decrease in pH causes `O_(2)` dissociation curve of haemoglobin to shift to
Last Answer : Decrease in pH causes `O_(2)` dissociation curve of haemoglobin to shift to A. shift of ... right C. remain unchanged D. will oscillate erratically
Description : Assertion `:-` Low concentration of oxygen allow dissociation of oxyhaemoglobin. Reason `:-` CO has more affinity with Haemoglobin as compares to oxyg
Last Answer : Assertion `:-` Low concentration of oxygen allow dissociation of oxyhaemoglobin. Reason `:-` CO has more ... D. If both Assertion & Reason are false.
Description : Body tissues obtain oxygen from haemoglobin because of its dissociation in tissues caused by
Last Answer : Body tissues obtain oxygen from haemoglobin because of its dissociation in tissues caused by A. Low ... concentration D. High `CO_(2)` concentration
Description : 2, 3-Biphosphoglycerate in high concentrations, combines with hemoglobin, causes (A) Displacement of the oxyhemoglobin dissociation curve to the left (B) Displacement of the oxyhemoglobin dissociation curve ... (C) No change in oxy hemoglobin dissociation curve (D) Increased affinity for oxygen
Last Answer : Answer : B
Description : Mast cells secrete (a) haemoglobin (b) hippurin (c) myoglobin (d) histamine
Last Answer : (d) histamine.
Description : Both Haemoglobin and myoglobin require _______ for formation —
Last Answer : Iron
Description : Oxygen dissociation curve shifts to right when `:-`
Last Answer : Oxygen dissociation curve shifts to right when `:-` A. `P_(o_(2))` decreases B. `P_(Co_(2))` decreases C. pH increases D. Temperature decreases
Description : The oxygen dissociation curve is shifted to the right with: a. polycythaemia b. pyrexia c. respiratory acidosis d. sickle cell anaemia
Last Answer : pyrexia
Description : A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition
Description : Assertion `:-` In the alveoli, dissociation of `CO_(2)` from carbamino-haemoglobin takes place Reason `:-` In the alveoli `P_(CO_(2))` is low and `P_(
Last Answer : Assertion `:-` In the alveoli, dissociation of `CO_(2)` from carbamino-haemoglobin takes place Reason ` ... . D. If both Assertion & Reason are false.
Description : Dissociation of `CO_(2)` from carbamino-haemoglobin takes place when:
Last Answer : Dissociation of `CO_(2)` from carbamino-haemoglobin takes place when:
Description : Bohr effect is (A) Shifting of oxyhemoglobin dissociation curve to the right (B) Shifting of oxyhemoglobin dissociation curve to the left (C) Ability of hemoglobin to combine with O2 (D) Exchange of chloride with carbonate
Last Answer : Answer : A
Description : In biological studies which of the following is used to refer to the oxygen-binding, iron-containing, conjugated protein complex present in the sarcoplasm of muscle cells? a) myelin b) myosin c) myoglobin d) none of these
Last Answer : ANSWER: C -- MYOGLOBIN
Description : The sigmoidal relationship between weed density and crop yield was proposed by a).Zimdahl 1980 b). Roberts and Bonds (1975) c). Cousens et al (1985) d). None of these
Last Answer : a).Zimdahl 1980
Description : Each myoglobin molecule contains (A) One iron atom (B) Two iron atoms (C) Four iron atoms (D) Six iron atoms
Description : About 5% of the total body, iron is present in (A) Transferrin (B) Myoglobin (C) Cytochromes (D) Haemosiderin
Description : Blood analysis of a patient reveals an unusually high quantity of carboxyhaemoglobin content. Which of the following conclusions is most likely to be correct? The patient has been inhaling polluted air ... content of (a) carbon disulphide (b) chloroform (c) carbon dioxide (d) carbon monoxide.
Last Answer : (d) carbon monoxide.
Description : Dissociation curve shifts to the right when
Last Answer : Dissociation curve shifts to the right when A. `CO_(2)` concentration decreases B. `CO_(2 ... increases D. `H^(+)` concentration decreases
Description : The dissociation curve is associated with
Last Answer : The dissociation curve is associated with A. Carbonic of erythrocytes B. Carbon dioxide C. Oxygen D. Oxyhaemoglobin
Description : `O_(2)` dissociation curve is:
Last Answer : `O_(2)` dissociation curve is:
Description : Methemoglobin is formed as a result of the oxidation of haemoglobin by oxidation agent: (A) Oxygen of Air (B) H2O2 (C) K4Fe(CN)6 (D) KMnO4
Last Answer : Answer : C
Description : When haemoglobin takes up oxygen there is a change in the structure due to the moving closer together of (A) β-chains (B) β-chains (C) γ-chains (D) α and γ chains
Description : Assertion `:-` In the tissue high `P_(O_(2))`, low `P_(CO_(2))`, higher `H^(o+)` concentration conditions are favourable for dissociation of oxygen fr
Last Answer : Assertion `:-` In the tissue high `P_(O_(2))`, low `P_(CO_(2))`, higher `H^(o+)` ... Reason is False. D. If both Assertion & Reason are false.
Description : The correct order in which oxygen - oxygen bond dissociation energy increases is:
Last Answer : The correct order in which oxygen - oxygen bond dissociation energy increases is: A. `H_(2)O_(2)ltO_(2)ltO_(3)` ... 2)` D. `O_(2)ltH_(2)O_(2)ltO_(3)`
Description : Ionisation energy of nitrogen is greater than that of oxygen because nitrogen has – (1) high bond dissociation energy (2) smaller atomic radius (3) stable half filled 2p sub level (4) high nuclear charge
Last Answer : (3) stable half filled 2p sub level Explanation: Ionization energy is a measure of the ease in which atoms lose electrons and become positive ions.
Description : Ionisation energy of nitrogen is greater than that of oxygen because nitrogen has (1) high bond dissociation energy (2) smaller atomic radius (3) stable half filled 2p sub level (4) high nuclear charge
Last Answer : stable half filled 2p sub level
Description : What is Myoglobin ?
Last Answer : Myoglobin is a type of protein linked by iron and oxygen. It is most commonly found in the fleshy muscle cells of vertebrates. It is related to hemoglobin.
Description : Myoglobin is present in
Last Answer : Myoglobin is present in A. White muscle fibers B. Red muscle fibers C. Involuntary muscles D. All the above
Description : The red colour of human blood is due to (1) myoglobin (2) hemoglobin (3) immunoglobulin (4) haptoglobin
Last Answer : (2) hemoglobin Explanation: Hemoglobin is the ironcontaining oxygen-transport metalloprotein in the red blood cells of all vertebrates which carries oxygen from the respiratory organs to the rest of the body. It ... oxygen than had in the vein the blood' came from. Therefore, the blood turns red.
Description : Mitotic spindle is mainly composed of which protein? (a) Actin (b) Myosin (c) Actomyosin (d) Myoglobin
Last Answer : c) Actomyosin
Description : The following protein/polypeptide has a quaternary structure : (A) cc-Chymotrypsin (B) Hemoglobin (C) Insulin (D) Myoglobin
Last Answer : (B) Hemoglobin
Last Answer : hemoglobin
Description : ___is rupture of red cells with release of intracellular haemoglobin can occur if the Antibody has the property of hemolysin. a) Agglutination b) Hemolysis c) Reaction
Last Answer : b) Hemolysis is the rupture of red blood cells with the release of intracellular hemoglobin, and it can occur if the antibody has the property of hemolysin. Hemolysis is the destruction or ... bacteria, and viruses, and it is a key principle in many diagnostic tests for infectious diseases.
Description : The enzyme amino acyl tRNA synthetase is involved in (A) Dissociation of discharged tRNA from 80S ribosome (B) Charging of tRNA with specific amino acids (C) Termination of protein synthesis (D) Nucleophilic attack on esterified carboxyl group of peptidyl tRNA
Description : The pH of an amino acid depends (A) Optical rotation (B) Dissociation constant (C) Diffusion coefficient(D) Chain length
Description : Carbon monoxide has how much greater affinity for haemoglobin as compared to oxygen? -Do You Know?
Last Answer : answer:
Description : Assertion `:-` Haemoglobin can not get saturated with oxygen more than `97%`. Reason `:-` With a rise in `PO_(2)`, the affinity between `O_(2)` & haem
Last Answer : Assertion `:-` Haemoglobin can not get saturated with oxygen more than `97%`. Reason `:-` With a ... False. D. If both Assertion & Reason are false.
Description : Binding of oxygen with haemoglobin is primarily related to `:`
Last Answer : Binding of oxygen with haemoglobin is primarily related to `:` A. Partial pressure of `O_(2)` B. ... ` C. `H^(+)` ion concentration D. Temperature
Description : Carbon monoxide has greater affinity for haemoglobin as compared to oxygen :
Last Answer : Carbon monoxide has greater affinity for haemoglobin as compared to oxygen : A. 1000 Times B. 200 Times C. 20Times D. 2 Times
Description : Determination of oxygen carried by haemoglobin is done by
Last Answer : Determination of oxygen carried by haemoglobin is done by A. pH B. Partial presure of oxygen C. Parital pressure of carbon D. All of above