Streptococci produce Select one: a. Hemoglobin b. Heme c. Hemolysin d. none
Streptococci produce Select one: a. Hemoglobin b. Heme c. Hemolysin d. none
Homework Answers
The answer is (c) Hemolysin
Streptococci produce Hemolysin.
- Hemolysis is the breakdown of red blood cells. It is mainly useful in the classification of the streptococcal species.
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Streptococci produce Select one: a. Hemoglobin b. Heme c.
Hemolysin d. none
2. The heme group found in hemoglobin is an example of which of the following? a....
2. The heme group found in hemoglobin is an example of which of the following? a. Metal ion b. Cosubstrate c. Coenzyme d. None of the above 3. A is altered in the course of the reaction and dissociates from the active site of the enzyme a. Casubstrate b. Prosthetic group c. Metal ion d. None of the above 4. NADH is an example of an a. Metal ion b. Organic cofactor c. Coenzyme d. B and C A catalytically...
2. The heme group found in hemoglobin is an example of which of the following? a....
2. The heme group found in hemoglobin is an example of which of the following? a. Metal ion b. Cosubstrate c. Coenzyme d. None of the above 3. A is altered in the course of the reaction and dissociates from the active site of the enzyme a. Cosubstrate b. Prosthetic group c. Metal ion d. None of the above 4. NADH is an example of an a. Metal ion b. Organic cofactor c. Coenzyme d. B and C A catalytically...
Which of the following statements is/are TRUE? Select one: O A. Heme is part of the...
Which of the following statements is/are TRUE? Select one: O A. Heme is part of the secondary structure of myoglobin. O B. The distal histidine assists in heme binding to myoglobin. O C. Oxygen binds to the proximal histidine. O D. All of the above statements are true O E. None of the above statements are true
Heme is the iron-containing structure in the proteins hemoglobin and myoglobin. In red blood cells, hemoglobin...
Heme is the iron-containing structure in the proteins hemoglobin and myoglobin. In red blood cells, hemoglobin enables oxygen uptake and transport. Myoglobin in muscle cells helps oxygen enter the cells. The oxygen carried by hemoglobin and myoglobin is critical for energy production. Because meat contains hemoglobin and myoglobin, beef, fish, and poultry contain more heme iron than most plant foods. The remaining iron in meat, as well as all the iron in vegetables, grains, dietary supplements, and fortified or enriched...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group 1. d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
Free heme regulates globin chain production by: Select one: O a. Activating heme-regulated inhibitor (HRD) of...
Free heme regulates globin chain production by: Select one: O a. Activating heme-regulated inhibitor (HRD) of translation O b. Inhibiting globin transcription O c. Increasing transcription of globin O d. Exerting a positive effect on heme-regulated inhibitor (HR) of translation Why does the reticulocyte production index (RPI) provide the best information about bone marrow response to anemia? Select one: a. RPI values will change quicker than a corrected reticulocyte count b. It will decrease in response to increased bone marrow...
SELECT ALL THAT APPLY. Which of the following atoms or molecules help comprise the heme center...
SELECT ALL THAT APPLY. Which of the following atoms or molecules help comprise the heme center of the proteins myoglobin and hemoglobin? A. Nitrogen B. Proximal Histidine C. Distal Histidine D. Oxygen
Hemoglobin: binds oxygen with a higher affinity than myoglobin due to the presence of four heme...
Hemoglobin: binds oxygen with a higher affinity than myoglobin due to the presence of four heme groups vs. only one in myoglobin. binds oxygen with a lower affinity than myoglobin due to the presence of four heme groups vs. only one in myoglobin. binds to oxygen with a lower affinity than myoglobin due to the presences of the T-state that is absent in myoglobin. binds to oxygen with a higher affinity than myoglobin due to the presences of the R-state...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix-...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin from its T-form to its R-form results in: a) Loss of BPG b) Does not result in release of CO2 c) cooperative...
Which statement is false about the heme group contained in globins? The chemical structure of the...
Which statement is false about the heme group contained in globins? The chemical structure of the heme groups in myoglobin and hemoglobin B The heme group is tightly, but non-covalently, held in myoglobin molecule. When oxygen binds to heme, the iron ion is oxidized from Fe to Fe3. If exposed to air, a free heme group (not associated with hemoglobin) is readily oxidized converting Fe2 to Fe3 and can no longer bind oxygen A are identical. C D
2. The heme group found in hemoglobin is an example of which of the following? a. Metal ion b. Cosubstrate c. Coenzyme d. None of the above 3. A is altered in the course of the reaction and dissociates from the active site of the enzyme a. Casubstrate b. Prosthetic group c. Metal ion d. None of the above 4. NADH is an example of an a. Metal ion b. Organic cofactor c. Coenzyme d. B and C A catalytically...
2. The heme group found in hemoglobin is an example of which of the following? a. Metal ion b. Cosubstrate c. Coenzyme d. None of the above 3. A is altered in the course of the reaction and dissociates from the active site of the enzyme a. Cosubstrate b. Prosthetic group c. Metal ion d. None of the above 4. NADH is an example of an a. Metal ion b. Organic cofactor c. Coenzyme d. B and C A catalytically...
Which of the following statements is/are TRUE? Select one: O A. Heme is part of the secondary structure of myoglobin. O B. The distal histidine assists in heme binding to myoglobin. O C. Oxygen binds to the proximal histidine. O D. All of the above statements are true O E. None of the above statements are true
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group 1. d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
Free heme regulates globin chain production by: Select one: O a. Activating heme-regulated inhibitor (HRD) of translation O b. Inhibiting globin transcription O c. Increasing transcription of globin O d. Exerting a positive effect on heme-regulated inhibitor (HR) of translation Why does the reticulocyte production index (RPI) provide the best information about bone marrow response to anemia? Select one: a. RPI values will change quicker than a corrected reticulocyte count b. It will decrease in response to increased bone marrow...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin from its T-form to its R-form results in: a) Loss of BPG b) Does not result in release of CO2 c) cooperative...
Which statement is false about the heme group contained in globins? The chemical structure of the heme groups in myoglobin and hemoglobin B The heme group is tightly, but non-covalently, held in myoglobin molecule. When oxygen binds to heme, the iron ion is oxidized from Fe to Fe3. If exposed to air, a free heme group (not associated with hemoglobin) is readily oxidized converting Fe2 to Fe3 and can no longer bind oxygen A are identical. C D
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