Week Six Flashcards
Knock It Out the Park Like Bruce
VBG vs. ABG
Allows for easier access, less pain and fewer complications associated with it.
- -> Venous - arterial PCO2, pH and HCO3- differ only in NARROW range.
- Venous PO2 DIFFERS GREATLY because normal level in tissues is 40 while arterial is 100 mmHG.
Metabolic Acidosis WITHOUT increased anion gap
Diarrhea
Carbonic Anhydrase Inhibitors
Renal tubular Acidosis
Hyperalimenation (IV feeding)
Metabolic Acidosis WITH increased anion gap
"MULEPAK" M: Methanol ingestion U: Uremia L: Lactic acidosis E: Ethylene glycol ingestion P: Paraldehyde ingestion A: Aspirin overdose K: Katoacidosis
Renal Maintenance of pH
- Regulation of plasma [HCO3-] - Kidney generates just enough bicarb to neutralize net acid production from metabolism.
- Excretes fixed metabolic acids (NH4+) and phosphoric acid (H2PO4-).
- Reabsorption of filtered bicarb in early PCT
Pulmonary Maintenance of pH
Balances CO2 excretion with metabolic CO2 production.
- Monitors arterial PCO2 by central chemoreceptors which will then increase or decrease alveolar ventilation depending on the level of arterial CO2.
Anion Gap
Indicates concentration of unmeasured anions such as protein, phosphate, sulfate and citrate.
- Help differentiate between metabolic acidosis cause by addition of acid or loss of HCO3-
Anion Gap = [Na+] - ([Cl-]+[HCO3-])
Buffer
Substance that can reversibly bind H+
- Provide limited but immediate limitations on pH change; resist changes to pH.
- Kidneys secrete and synthesize HCO3- as buffering system.
3 Ways CO2 is Carried in Lungs for Expiration
- Bicarbonate - majority
- Bound to protein (esp. Hgb)
- Dissolved in plasma (CO2, 20 times more soluble than O2)
CO2 + H2O ⇄ H2CO3 ⇄ (H+) + HCO3-
enzyme = carbonic anhydrase
Erythropoietin
Glycoprotein growth factor that promotes differentiation of proerythroblasts into RBCs.
- Induced in kidney in response to hypoxia.
OxyHgb Dissociation Curve: Shifts to RIght
Decrease of Hgb to O2 –> Increases p50 –> Unloading of 02 in tissues is facilitated
a. Increased PCO2, decreases pH
b. Increases Temperature
c. Increases 2,3-DPG (increases hypoxic conditions such as high altitudes to facilitate delivery of O2 to tissues as an adaptive mechanism.
RELEASE O2
OxyHgb Dissociation Curve: Shifts to Left
Increase of Hgb for O2 –> p50 –> Unloading of O2 in tissues is difficult (binding of O2 is tighter)
a. Decreases PCO2, increases pH
b. Decreases pH
c. Decreases 2-3-DPG
d. Hgb F
e. Carbon monoxide - has higher affinity for Hgb than O2
Loves O2
p50
PO2 at which Hgb is 50% saturated (2/4 heme sites bound to O2)
- Decrease in p50 –> affinity for 02 increases - O2 bound more tightly to Hgb.
- Increase in p50 –> affinity for O2 decreases - Frees up O2 from Hgb.
OxyHgb Dissociation Curve
Sigmodal shape –> positive cooperativity
- binding of 1st molecule of O2 to heme group increases affinity for second and so forth
- Body able to tolerate changes in PaO2-O2 has highest affinity for Hgb.
- Very small changes in PaO2 will affect O2 affinity for Hgb –> causing big changes in Hgb saturation.
See Note Card for Respective graph
O2 Content
Actual amount of O2 per volume of blood.
- Includes dissolved O2 and O2 bound to Hgb
- O2 bound = O2 capacity of Hgb x % Hgb saturation
- Dissolved O2 = PaO2 x ((0.003 mL O2/mmHg)/(100mL blood))
- O2 bound + dissolved O2 = Total O2 content
Hgb Saturation
Amount of heme groups on each molecule of Hgb that are bound to oxygen
100% saturation = all 4 Heme groups on each Hgb molecule are bound to oxygen
% Hgb saturation = ((O2 bound to Hgb)/(O2 capacity of Hgb)) x 100%