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93 Cards in this Set
- Front
- Back
Acidosis |
Increase in the acidity of the blood due to excessive loss of bicarbonate |
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Alkalosis |
Increased in blood alkalinity due to accumulation of alkaline or reduction in acid |
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Allosteric |
Charge which alters functioning of the organism or molecule |
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Amino Acid |
One of a large group of organic compounds marked by the presence of both an amino group (NH3) and carboxyl group (COOH); the building protein |
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Complement |
A group of protein which plays vital role in the bodes defenses through a series of carefully orchestrated reactions |
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Cyanosis |
Blue tinge to the extremities -fingers, toes, lips |
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Hyperplasia |
Excessive proliferation of normal cells in the normal tissue of an organ |
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Polychromasia |
Blue tinge to the red cells indicating premature disease
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Which of these hemoglobins is an embryonic hemoglobin?
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Hgb Gower |
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How many total genes does a person posses for the production of alpha chains?
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4 (Four) |
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Name one condition that may shift the OD curve to the left. |
Anemia |
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If polychromasia is increased in the peripheral smear, the _________ should be elevated. |
Reticulocyte Count |
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IF 2, 3-DPG increases, the hemoglobin molecule releases more oxygen. This is known as a _______OD curve. |
Right - Shifted OD Curve |
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Which of the following statements regarding 2,3-DPG is correct? |
It controls hemoglobin affinity for oxygen |
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When the iron in the hemoglobin molecule is in the ferric(Fe^3+) state, hemoglobin is termed?? |
Methemoglobin |
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What percent of hemoglobin is synthesized in the reticulocyte stage? |
35 % |
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Epsilon and zeta chains are part of which of the flowing hemoglobin? |
Hgb Portland |
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Fetal hemoglobin consist of which of the following chains? |
a2E2 (a-aplha)
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Hemoglobin Molecules Consist of 2 primary structures |
1. Heme Portin 2. Globin Portin
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Define Hemoglobin |
Life giving structure of every red blood cells, the oxygen-carrying component of the red blood cells.
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What is consist of the Heme portion? |
- 4 iron atoms Fe2+ -Iron is surrounded by each protoporphyrin ring |
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What is consist of the Globin portion? |
Two pairs of polypeptide chains ---Normal postnatal hemoglobin is made of ---Two alpha chains (a) and two beta (b) chains ---Two alpha chains (a) and two delta (d) chains ---Two alpha chains (a) and two gamma (y) chains
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Hemoglobin Composition- Heme |
* The iron is surrounded by protoporphyrin IX or the porphyrin ring |
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Globin portion |
* Consists of amino acids linked together to form a polypeptide chain |
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Hemoglobin Forms |
* Each globin chain is under the influence of a specific chromosome |
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3. Adult Hemoglobin |
* Hemoglobin A (α2 β2): 96%–98% (majority of adult hemoglobin) |
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Hemoglobin function |
* Oxygen delivery is the principal purpose of the hemoglobin * Hemoglobin also transports C02 away from the tissues * The hemoglobin molecule loads oxygen on a one-to- one basis * one molecule of oxygen to one molecule of heme in the oxygen-rich environment of the lungs * As hemoglobin goes through the loading and unloading process, changes occur in the molecule * allosteric changes |
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Hemoglobin function |
* The hemoglobin molecule takes a tense and a relaxed form * When tensed * hemoglobin is not oxygenated * 2,3-DPG is at the center of the molecule * salt bridges between the globin chains are in place * When relaxed * hemoglobin is oxygenated * 2,3-DPG is expelled * salt bridges are broken * molecule is capable of fully loading oxygen |
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Oxygen Dissociation (OD) Curve |
* Hemoglobin delivers oxygen in exchange for CO2 * OD curve represents oxygen release from hemoglobin to the tissues * Sigmoid shape * Increase bound oxygen when Increase PO2 * Lungs: PO2 is 100 mm Hg = 97% Hgb saturation * Circulation: PO2 is 40 mm Hg = 25% Hgb saturation |
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Oxygen Dissociation (OD) Curve |
* In the normal curve (blue) at 40 mm Hg, 75% of the hemoglobin molecule is saturated with oxygen, leaving 25% capable of being released to tissue (7.4) * For the right shifted curve (red), at 40 mm Hg, hemoglobin is 50% saturated but willing to give up 50% of its oxygen to the tissues (7.2) * For the left shifted curve (green), at 40 mm Hg, hemoglobin is 85% saturated but willing to release only 12% to the tissues. (7.6) |
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OD Curve Changes Shift to the Right |
* Shift to right * More likely to release oxygen to tissue * Lower affinity * Anemia * Acidosis (Decreased pH) * Increased 2,3-DPG * Elevated body temperature (fever) |
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OD Curve Changes Shift to the Left |
* Shift to left * Less likely to release oxygen to tissue * Higher affinity * Abnormal hemoglobin * Alkalosis (Increased pH) * Decrease 2,3-DPG, body temp, and abnormal Hgb (CO) |
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Abnormal Hemoglobin |
* Hemoglobins that are physiologically abnormal have a higher oxygen affinity |
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Abnormal Hemoglobin |
* 2. Sulfhemoglobin * Exposure to sulfonamides * sulfemoglobin cannot carry oxygen * It may be toxic at low levels * 3. Carboxyhemoglobin * High affinity for carbon monoxide * Affinity is 200 times greater than its affinity for oxygen; * no oxygen is delivered to the tissues |
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Hemolysis |
* Red blood cell death is a natural process after 120-days
* The contents of the RBC are released and recycled for RBC regeneration * If premature cell death or hemolysis occurs, a series of events begin to cascade providing laboratory evidence that cells are dying earlier than 120-day life cycle * The bone marrow shows erythroid hyperplasia * increase in red blood cell precursors * premature release of reticulocytes and other immature cells * The peripheral smear provides visual clues of hemolysis * increase in polychromasia * presence of nucleated red blood cells * spherocytes |
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Hemolysis |
* Extravascular 90%
* RES system: spleen, liver, lymph nodes, bone marrow * Releases heme and globin contents to be recycled * Iron is transported via transferrin to the bone marrow or storage sites to be used in erythropoiesis * Rest of hemoglobin molecule reacts with hemoxygenase, yielding- biliverdin * biliverdin is reduced to unconjugated bilirubin * This bilirubin product attaches to albumin and is transported to the liver * Intravascular * Lysed directly in blood vessels * Table 4.2 p. 55 * Extravascular hemolysis: increased * bilirubin, decreased haptoglobin |
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Hemolytic Anemia: Intravascular |
* Decrease Hgb, HCT, RBC count
* Increase Serum bilirubin * Decrease Serum haptoglobin * Hemoglobinemia (free Hgb) * Hemoglobinuria * Possible Increase retic * Increase LDH * Schistocytes |
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Hemolytic Anemia: Extravascular |
* Decrease Hgb, HCT, RBC count |
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Intrinsic Red Cell Defects leading to hemolysis (anemia) |
* Hemoglobinopathies
* Structural and synthesis * Red cell membrane defects * Red cell enzyme defects * Stem cell defects |
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Extrinsic Red Cell Defects |
* Autoimmune hemolytic anemia (AIHA)
* Parasitic infections * Microangiopathic hemolytic anemia (MHA) * caused by factors in the small blood vessels * Environmental agents * Venoms * Chemical agents |
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Amino Acids |
Alpha Chains -141 Amino Acids in a unique arrangement. Beta Chains - 146 Amino Acids in a unique arrangement. |
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2,3-DPG |
A substance produced via the Embden Meyerhof pathway during anaerobic glycolysis. This structure relates to oxygen affinity of hemoglobin. |
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Synthesis of Hemoglobin |
Hemoglobin synthesis begins at Polychromatic normoblast stage of RBC development. this synthesis is seen by the change in cytoplasmic color from a deep blue to lavender cytoplasmic color. Hemoglobin, 65% is synthesized before the RBC nucleus is extruded, with an additional 35% synthesis by reticulocyte stage. |
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Normal Mature RBC |
Full complement of hemoglobin which occupies a little less than one-half of the surface area of the RBC. |
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Epsilon and Zeta Chains reserved for the what production? |
Production of Embryonic Hemoglobin |
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Embryo Develops |
Hgb Gower 1 (a2, E2) (Alpha 2, Epsilon 2) |
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Synthesized and remain in Embryo for 3 months |
Hgb Portland (y2$2) These hemoglobin do not participate in oxygen delivery |
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Fetal Hemoglobin |
Hgb F (a2y2)(alpha2,gamma2) Being to synthesized at 3 months of Fetal development and remains as the majority hemoglobin at birth |
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3 to 6 months after delivery |
Hgb A (alpha2, beta 2) The amount of gamma chains declines and the amount of beta chains increases. Hgb A, the majority of adult hemoglobin (95-98%) |
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Hemoglobin consist of ? |
Iron and Protoporhyrin Ring |
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Globin consist of? |
Amino acid chains of specific lengths and specific amino acidosis. Alpha and Beta are the two most significant amino acid chains. |
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What are the 2 Embryonic Hemoglobin? |
Hgb Gower and Hgb Portland |
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What is the Fetal Hemoglobin? |
Hgb F |
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Adult Hemoglobin? |
Hgb A - Primary Hgb A2 and Hgb F - Complement |
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Oxygen Delivery? |
Primary purpose of Hemoglobin molecule |
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2,3-DPG |
Related to oxygen affinity of hemoglobin |
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OD Curve Represents? |
The saturation of hemoglobin with oxygen and the release of oxygen from the hemoglobin molecule under normal and abnormal physiologic conditions.
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Hemolysis |
Is the premature destruction of the RBC before 120 day life cycle |
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Hemolysis Classified as? |
Intravascular or Extravascular , which relates to the site of hemolysis |
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Intravascular Hemolysis |
Occurs inside the body vessels |
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Extravascular Hemolysis |
Occurs outside the body vessels, primarily in the reticuloendothelial system |
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Hemolyic Anemias |
Classified by intrinsic defects of RBC or extrinsic defects that affects the RBCs. |
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Name 4 microcytic anemias: |
1. Iron deficiency anemia (IDA) |
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Two ways that IDA (iron deficient anemia) can develop |
1. deficient iron intake |
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What causes thalassemia |
1. Caused by missing or diminished alpha or beta globin chains |
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Describe iron overload disorders |
1. Ex: hereditary hemochromatosis |
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What causes anemia of chronic disorders |
1. arises from renal failure or thyroid dysfunction |
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Conditions that cause macrocytes: |
1. liver disease of alcoholism |
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Describe appearance of Spherocytes |
They are dense, dark red and small |
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What are the three major parts of a hemoglobin molecule |
1. Heme |
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How may molecules of iron per heme? |
4 iron atoms (Fe2+) |
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Name the three types of synthesized hemoglobin |
1. embryonic hemoglobin |
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Name the thee types of adult hemoglobin and its percentages |
Hemoglobin A (95 - 98%) |
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Main function of hemoglobin |
Principal purpose is oxygen delivery |
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Explain Oxygen dissociation curve |
1. S-shaped |
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In lungs if PO2 is 100 mm Hg then hemoglobin will be ___ % saturation |
97 |
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Shift to right |
more likely to release oxygen to tissue |
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Shift to left |
Less likely to release oxygen to tissue |
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Name the three types of abnormal hemoglobin |
These are often formed by accidental or intentional ingestion or they can be inherited defects |
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Two types of hemolysis |
1. extravasular |
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Extravascular hemolysis |
red blood cells are lysed in organs |
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Intravascular hemolysis |
red blood cells are lysed directly into the blood |
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In venous circulation if PO2 is 40 mm Hg then hemoglobin saturation is ___ saturation |
75% |
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Which of these hemoglobins is an embryonic hemoglobin
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Hgb Gower |
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How many total genes does a person posses for the production of alpha chain |
4 |
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Name one condition that may shift the OC curve to the left |
Inheriting a high oxygen affinity hemoglobin |
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If polychromasia is increased in the peripheral smear, the ------should be elevated |
Reticulocyte count |
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If 2,3-DPG increases, the hemoglobin molecule releases more oxygen. |
This is known as a Right-shifted |
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which of the following statements regarding 2,3-DPG is correct? |
It controls hemoglobin affinity for oxygen |
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When the iron in the hemoglobin molecule is in the ferric (Fe3+) state, hemoglobin is termed
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Methemoglobin |
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What percent of hemoglobin is synthesized in the reticulocyte stage
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35% |
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Epsilon and zeta chains are part of which of the following hemoglobin
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Hgb Portland |
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Fetal hemoglobin consists of which of the following chain?
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(alpha2, gamma2) or (a2,Y2) |