The 'Pace quiz Sem 1, Blood Quiz' assesses knowledge on key hematological components such as eosinophils, lymphocytes, thromboxane, and antithrombin III. It evaluates understanding of platelet function, thrombin regulation, and their impacts on vascular and immune responses, crucial for medical and biological studies.
Neutrophil
Eosinophil
Monocyte
Lymphocyte
Basophil
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Haptoglobin
Hemopexin
Transferrin
Alphal-antitryptsin
Hemoglobin
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Lymphocyte
Neutrophil
Monocyte
Basophil
Neutrophil
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The hemophilia A patient
The hemophilia B patient
Both
Neither
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Myoglobin undergoes a conformational change that raises its oxygen affinity above that of hemoglobin
2,3BPG dissociates from hemoglobin and binds to myoglobin.
Much more of the dissolved oxygen binds to myoglobin than to hemoglobin.
Hemoglobin dissociates into its subunits
Most of the hemoglobin becomes oxygenated while most of the myoglobin rema ins deoxygenated
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Oxygen binds to Fe+3 but not to Fe+2.
Hydrophobic interactions are the primary forces associated with BPG bind ing to hemoglobin
When oxyhemoglobin moves to a more acidic environment, it is more apt to release its oxygen
Carbon dioxide binds to Fe+2 but not to Fe+3 hemoglobin
Carbon monoxide binds to Fe+3 but not to Fe+2 hemoglobin.
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Platelet aggregation and leukocyte adhesion
Secretion of prostaglandins from endothelial cells
Secretion of thrombin from leukocytes
Formation of fibrin monomer
Contact phase activation
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Prevent the hormones from being excreted in the urine
Make the hormones soluble in an aqueous phase
Prevent degradation of the hormones in the vascular system
Keep the hormones in an inactive state until they are delivered to the target tissue
Have receptors on all body cells
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Is more hydrophllic than hemoglobin A
Is more hydrophobic than hemoglobin A
Has a different number of electrical charges than hemoglobin A
Has a more compact shape than hemoglobin A
Has a different molecular weight than hemoglobin A
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Lack of erythropoietin
Excessive formation of fibrin clots caused by excessive sickling
Acute iron deficiency
Trapping of erythrocytes in the spleen
Internal bleeding
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Yes, but only with two different fathers
No, there has to be an error in the blood type for the daughter
Yes, the father must have been BO and Rh-/Rh- homozygote
Yes, the father must have been BO or AB with one allele Rh-
Yes, the father must have been BO and Rh+
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Serotonin
Phosphatidyl inositol
Thromboxane
Prostaglandins
Leukotrienes
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The tenase complex
Stabilization of factor VIII
Release of bradykinin from high molecular weight kininogen
Lipid associated coagulation inhibitor
Fibrinolysis
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Factor VIla
Factor IXa
Fibrin
Antithrombin III
Factor VIlla
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Serotonin
Phosphatidyl inositol
Thromboxane
Prostaglandins
Leukotrienes
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Factor V
Factor VIII
Factor II
High molecular weight kininogen
Von Willebrand factor
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Gamma-glutamyltransferase (GGT)
Alkaline phosphatase
Lactate dehydrogenase
Acid phosphatase
Alanine transaminase
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Amino acid substitutions in the galactosyl transferase
Inactivation of the Fucose transferase
Frameshift mutation in the galactosyl transferase
Differential ability to produce sugars D-galactose or N-acetylgalactosamine
Expression of Fucose transferase type 1 versus type 2 leading to use of different substrate structures
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Sickle cell disease or a-thalassemia but not B-thalassemia
A-thalassemia but not sickle cell disease or B-thalassemia
Sickle cell disease or B-thalassemia but not a-thalassemia
Sickle cell disease but not a-thalassemia or B-thalassemia
A-thalassemia or B-thalassemia but not sickle cell disease
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Allelic heterogeneity
Locus heterogeneity
Epistasis
Skewed X-inactivation
Multiple call inearity
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