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Download MBBS Biochemistry PPT 14 Oxygen Dissociation Curve And Its Clinical Importance Lecture Notes

Download MBBS (Bachelor of Medicine, Bachelor of Surgery) 1st year (First Year) Biochemistry ppt lectures Topic 14 Oxygen Dissociation Curve And Its Clinical Importance Notes. - biochemistry notes pdf, biochemistry mbbs 1st year notes pdf, biochemistry mbbs notes pdf, biochemistry lecture notes, paramedical biochemistry notes, medical biochemistry pdf, biochemistry lecture notes 2022 ppt, biochemistry pdf.

This post was last modified on 05 April 2022

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Case

? 49-year-old man who was admitted to the department of chest

medicine with dyspnea, weakness and cyanosis in whom differential

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diagnosis excluded acute and chronic pulmonary and cardiovascular

disease.

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? Saturation measured with a finger pulse oximeter was 89%.
? Despite administration of oxygen through a nasal cannula, saturation

measured with a pulse oximeter did not change.
? Arterial blood gas analysis revealed a saturation of 97.9%, PaO 2 of 102

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mm Hg, PaCO2 of 35 mm Hg, HCO3 of 3.4 mmol/l, pH of 7.44.

? Clinical cyanosis and low measured oxygen saturation in the presence

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of normal arterial oxygen tension was highly suggestive of

methemoglobinemia ("saturation gap").

? Methemoglobin level, measured at the acute phase of disease was

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elevated at 16%. Episode resolved spontaneously.

Saturation Gap

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? The "oxygen saturation gap" is the difference between the calculated

oxygen saturation from a standard blood gas machine and the reading

from a pulse oximeter.

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? If it is greater than 5%, the patient's hemoglobin may be abnormal,

representing carbon monoxide poisoning, methemoglobinemia, or

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sulfhemoglobinemia.

? In present case(97.9%- 89%= 8.9%)
Pulse Oximetry

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(measured oxygen saturation
? Pulse oximetry is based on measurement of a ratio of light absorption

by tissues at a red wavelength (660 nm) and at an infrared

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wavelength (940 nm).

? OxyHb absorbs infrared and deoxyHb absorbs red light

? Uses empirically derived calibration curves that converts ratio of oxy

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to deoxyHb into %saturation.

Calculated oxygen saturation(ABG Machine)

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? Calculates % oxygen saturation by following formula

sO2(%) = cHbO2/cHbo2+cHHb
? It is important to note that the denominator in this equation is not

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the concentration of total hemoglobin.

? There are two species of hemoglobin present in blood that are

incapable of binding oxygen. They are carboxyhemoglobin (COHb)

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and methemoglobin (MetHb)

? In health, COHb and MetHb together comprise less than ~5 % of total

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hemoglobin so that, normally, the concentration of total hemoglobin

(ctHb) approximates to the sum of cO 2Hb and cHHb.

? However, there are pathologies ? most notably carbon monoxide

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poisoning and methemoglobinemia ? that are associated with a

marked increase in COHb or MetHb, and a resulting marked reduction

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in the oxygen-carrying capacity of blood, that is not reflected in sO 2.

This results in "Saturation Gap"
Co-Oximeter

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? Many modern blood gas analyzers have an incorporated CO-oximeter

? The measurement is based on spectrophotometric analysis of the

hemoglobin released from a sample of arterial blood

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? The four hemoglobin species present in blood (oxyhemoglobin, O 2Hb;

deoxyhemoglobin, HHb; carboxyhemoglobin, COHb; and

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methemoglobin, MetHb) each have a characteristic light-absorption

spectrum.

Relationship of O2 saturation with pO2

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? A number of environmental factors in blood determine the relative

affinity of hemoglobin for oxygen. The most significant of these

is pO 2.

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? Hemoglobin present in blood with relatively high pO 2 has much

greater affinity for oxygen than hemoglobin present in blood with

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relatively low pO 2.

? The oxygen dissociation curve (ODC) describes this relationship

graphical y (sO 2 denotes Hb affinity)

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Oxygen Hemoglobin Dissociation curve

Although pO 2only reflects a very small proportion (3 %) of the oxygen in

arterial blood, it is highly significant because, as the ODC implies,

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it determines the sO 2 and therefore the total amount of oxygen

that is contained in arterial blood for delivery to tissues.

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Factors affecting ODC

1. Carbon dioxide
2. Protons (pH)
3. Temperature

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4. 2,3 BPG

Increase in any of the above shifts

curve to right and vice-versa

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Bohr Effect

? The Bohr effect is decreased affinity of hemoglobin for oxygen with

increase in H+ or CO2

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H+

CO2

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O2

O2

O2

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Importance of Bohr Effect

? Bohr Effect shifts ODC to right

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increasing oxygen delivery
Bohr Effect and

Haldane Effect

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Methemoglobinemia

(Discussion of case)
? Cyanosis(chocolate cyanosis) with structural y normal heart.
? Important D/D for an acquired or drug induced cause

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? Hemoglobin can accept and transport oxygen only when the iron

atom is in its ferrous form

? When haemoglobin becomes oxidized, the iron atom is converted to

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the ferric state (Fe3+), resulting in the formation of methemoglobin

? Methemoglobin lacks the electron that is needed to form a bond with

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oxygen and thus is incapable of oxygen transport.
? The low level of methemoglobin is maintained through 2 important

mechanisms

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1. HMP shunt pathway within the erythrocyte. Through this pathway,

oxidizing agents are reduced by glutathione.

2. Enzyme cytochrome b5 reductase(Methemoglobin reductase) , requires

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NADH to reduce methemoglobin to its original ferrous state.

? Any drug that interferes with these mechanisms can lead to

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Methemoglobinemia

Conversion Of Methemoglobin To

Hemoglobin is

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NADPH+H+ Dependent

H2O2 and Oxidant Drugs

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Methemoglobin

Hemoglobin (Fe+2)

(Fe+3)

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Methemoglobin Reductase

NADP+

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NADPH+ H+
? Congenital Methemoglobinemia
1. arises from globin mutations that Stabilize iron in the ferric state (e.g.

HbM Iwata [87HisTy]

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2. from mutations that impair the enzymes that reduce methemoglobin

to hemoglobin (e.g.methemoglobin reductase, NADP diaphorase).

? Acquired Methemoglobinemia is caused by toxins that oxidize heme

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iron notably nitrate and nitrite-containing compounds including

drugs commonly used in cardiology and anesthesiology.

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Management of Methemoglobinemia

Diagnosis
? Arterial blood with elevated methemoglobin levels has a

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characteristic chocolate-brown color(chocolate cyanosis)

? Saturation Gap
Treatment
? Intravenous (IV) methylene blue is the first-line antidotal agent.

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? Exchange transfusion and hyperbaric oxygen treatment are second-

line options for patients with severe methemoglobinemia
Therapeutic Induction of Methemoglobin

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Formation

? Cyanide competes with cytochrome

oxidase for Fe+++ of methemoglobin to

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form cyanmethemoglobin which is

eliminated

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? Thereby, the activity of inhibited

cytochrome oxidase is restored.

? Agents used as antidote: sodium nitrite,

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amyl nitrite, 4-dimethylaminophenol

Minor Hb

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ODC with different types of Hb and Mb

HbF( Fetal Hemoglobin)
? Binding of 2,3-BPG to HbF: weak

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? ? Importance

? Residue H21 of the subunit of HbF is Ser rather than His. Since Ser cannot

form a salt bridge, BPG binds more weakly to HbF than to HbA.

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? The higher oxygen affinity of HbF facilitates the transfer of oxygen from the

maternal circulation across the placenta to the RBC of the fetus.

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HbA1c

ADA Criteria for Diabetes Mel itus

HbA1c > 6.5%

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HbA1c

? A1C reflects average glycemia over approximately 3 months and has

strong predictive value for diabetes complications

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? A1C testing should be performed routinely in all patients with

diabetes--at initial assessment and as part of continuing care

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? Factors affecting HbA1c measurement:
1. Glucose concentration
2. Red cell turnover
3. Analytical Variations

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Diabetes Care 2018;41(Suppl. 1):S55?S64

HbA1c
? Variations by Variable Red cell Turnover: hemolytic and other

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anemias, recent blood transfusion, use of drugs that stimulate

erythropoesis, end-stage kidney disease, and pregnancy

Methods:

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? Ion-exchange high-performance liquid chromatography (HPLC),
? Boronate affinity assay,
? Immunoagglutination
Ref Range: 4-6.2%
Myoglobin

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Why is myoglobin unsuitable as an O 2 transport

protein but wel suited for O 2 storage?
S.No Hemoglobin (Hb)

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Myoglobin (Mb)

1.

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Hb is Oxygen transport protein in Mb is Oxygen storing protein in

RBCs of blood.

muscles.

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2.

Tetrameric has four Heme and

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Monomeric has one Heme and binds

binds with 4O2

with 1 O2.

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3.

Oxygenated at Lungs

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Oxygenated at Muscle Cel Cytosol.

4.

HbO2 unloads oxygen at tissues

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MbO2 unloads oxygen at cell cytosol

when pO2 is at 40 mmHg.

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when pO2 is at 5 mmHg. to rapidly

respiring cells

P50 for HbA1 is 27 torr.

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P50 for Mb is 2 torr.

5.

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ODC is sigmoid shaped

ODC is hyperbolic shaped.

6.

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Hb has 574 amino acids.

Mb has 153 amino acids.

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Mol .wt-67,000 Daltons.

Mol wt-17,200 Daltons.

?Thank You!

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