2- Biochemistry Of Blood Tissue Flashcards

(54 cards)

1
Q

What are the basic functions of blood?

A
  • Respiration
  • Alimentation
  • Removal of waste
  • Buffering
  • Osmotic balance
  • Body temperature regulation
  • Immunologic defense
  • Coagulation
  • Transport hormones and metabolites

These functions are essential for maintaining homeostasis and supporting life processes.

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2
Q

What is the composition of whole blood?

A
  • Plasma: 55%
  • Buffy Coat: <1%
  • Erythrocytes: 45%

Plasma is the liquid medium of blood, while erythrocytes are red blood cells responsible for oxygen transport.

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3
Q

What is the primary component of blood plasma?

A

92% water

8% Plasma also contains proteins and trace amounts of :
Blood clotting factors, immunoglobins ( antibodies ), lipoprotein particles and electrolytes ( mainly sodium and chloride )

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4
Q

What is the normal pH range of blood?

A

7.35 – 7.45

This pH range is crucial for proper physiological function.

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5
Q

What are the main types of plasma proteins?

A
  • Albumin
  • α1-globulins
  • α2-globulins
  • β-globulins
  • γ-globulins
  • Both solubility and electrophoretic migration rates of globulins are lower
    than albumin.
  • These proteins serve various functions including transport, immunity, and maintaining osmotic pressure.
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6
Q

What is the function of albumin in blood plasma?

A
  • Transport of fatty acids, bilirubin, steroid hormones, vitamins, and drugs
  • Maintenance of oncotic pressure
  • Acts as a buffer

Albumin constitutes about 60% of all plasma proteins.

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7
Q

True or False: Most plasma proteins are synthesized in the liver.

A

True

Over 90% of plasma proteins originate from the liver, with some exceptions like immunoglobulins.

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8
Q

Fill in the blank: The half-life of albumin in blood is ______.

A

20 days

This long half-life contributes to albumin’s stability in circulation.

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9
Q

What role do α1-globulins play in the body?

A
  • Inhibit proteases
  • Act as acute phase reactants
  • Transport cortisol and other substances

Examples include alpha-1-antitrypsin and prothrombin.

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10
Q

What is the main function of haptoglobin?

A

Binding of free hemoglobin

Haptoglobin helps to prevent kidney damage by binding free hemoglobin released from red blood cells.

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11
Q

What are γ-globulins primarily known for?

A

Immunoglobulins (antibodies)

They play a crucial role in the immune response by identifying and neutralizing pathogens.

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12
Q

What is the significance of ceruloplasmin in blood?

A

Transport of copper ions

Ceruloplasmin contains six copper atoms per molecule and is important for iron metabolism.

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13
Q

What condition is associated with α1-antitrypsin deficiency?

A

Emphysema and liver disease

This deficiency can lead to unchecked activity of neutrophil elastase, damaging lung tissue.

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14
Q

What is the role of transferrin in blood plasma?

A

Transport of iron ions

Transferrin is crucial for iron homeostasis in the body.

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15
Q

What is the primary role of immunoglobulins?

A

Defense against infections

They identify and neutralize foreign objects like bacteria and viruses.

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16
Q

How is protein electrophoresis used in laboratory settings?

A

To separate proteins in serum and body fluids into component albumin and globulins.

This technique helps in diagnosing various diseases by analyzing protein patterns.

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17
Q

What is the function of fibrinogen in blood?

A

Coagulation factor I

Fibrinogen is converted into fibrin during blood clotting, essential for wound healing.

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18
Q

What are the five types of immunoglobulins?

A

IgG, IgA, IgM, IgD, IgE

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19
Q

What is the main antibody in the secondary response?

A

IgG

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20
Q

Which immunoglobulin crosses the placenta?

A

IgG

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21
Q

What is the primary function of secretory IgA?

A

Prevents attachment of bacteria and viruses to mucous membranes

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22
Q

Which immunoglobulin acts as an antigen receptor on B cells?

23
Q

Which immunoglobulin is involved in allergic responses?

24
Q

What is the structure of immunoglobulins?

A

Y-shaped, with two heavy chains and two light chains

25
What are the common light chains found in all immunoglobulin types?
κ (kappa), λ (lambda)
26
What is the role of acute-phase proteins?
Increase or decrease in plasma concentration in response to inflammation
27
Name two positive acute-phase proteins.
* CRP * Haptoglobulin
28
What is the third most abundant body protein?
Hemoglobin
29
What is the composition of hemoglobin?
4 globin chains: 2 alpha and 2 beta
30
How many oxygen molecules can hemoglobin bind?
4
31
What is the significance of cooperative binding in hemoglobin?
Hb’s affinity for O2 increases as its O2 saturation increases
32
What does the oxygen dissociation curve (ODC) illustrate?
How blood carries and releases O2
33
What is the P50 value in relation to hemoglobin?
Partial pressure of O2 at which red blood cells are 50% saturated with O2
34
What effect does an increase in P50 indicate?
Decreased affinity for O2
35
What factors can cause a right shift in the oxygen dissociation curve?
* Increase in PCO2 * Increase in temperature * Decrease in pH * Increase in 2,3-DPG concentration
36
What is the Bohr effect?
Decreased O2 affinity of Hb allowing more O2 release to tissues
37
What is the role of 2,3-bisphosphoglycerate (2,3-BPG)?
Decreases hemoglobin’s oxygen affinity
38
How is CO2 transported in the blood?
* 7-10% dissolved in plasma * 10-15% as carbaminoHb * ~80% as bicarbonate ions (HCO3-)
39
What happens to hemoglobin when it binds CO2?
It stabilizes the T (tense) form, resulting in decreased O2 affinity
40
How do CO2 levels affect the oxygen dissociation curve?
Increase in CO2 causes a right shift; decrease in CO2 causes a left shift
41
What color does carbaminohemoglobin exhibit, and what is its significance?
Distinctive blue color contributing to the appearance of deoxygenated venous blood
42
What is carbaminohemoglobin and its color?
Carbaminohemoglobin has a distinctive blue color that may contribute to the dark red color of deoxygenated venous blood ## Footnote It is compared to the bright, saturated red of oxygenated arterial blood.
43
What is cyanosis?
Cyanosis is high levels of deoxyHb in blood caused by decreased oxygenation of tissues ## Footnote It develops when arterial oxygen saturation drops below 85% or 75%.
44
How does temperature affect the oxygen dissociation curve (ODC)?
An increase in temperature shifts the curve to the right, while a decrease shifts it to the left ## Footnote Increasing temperature denatures the bond between O2 and hemoglobin, increasing O2 release.
45
What is methemoglobin?
Methemoglobin is an abnormal form of hemoglobin where the ferrous (Fe++) form is converted to the ferric (Fe+++) state ## Footnote It causes a left shift in the curve as methemoglobin does not unload O2.
46
How does carbon monoxide affect oxygen transport?
Carbon monoxide interferes with oxygen transport by forming carboxyhemoglobin (COHb) ## Footnote CO has approximately 240 times the affinity for hemoglobin that oxygen has.
47
What is fetal hemoglobin (HbF)?
Fetal hemoglobin is the main oxygen transport protein in the human fetus during the last 7 months of development ## Footnote It has a different composition than adult hemoglobin, allowing for greater affinity for oxygen.
48
How does fetal hemoglobin differ from adult hemoglobin?
Fetal hemoglobin is composed of two alpha and two gamma subunits, while adult hemoglobin consists of two alpha and two beta subunits ## Footnote This results in a left-shifted oxygen dissociation curve for fetal hemoglobin.
49
What is myoglobin (Mb)?
Myoglobin is a globular heme pigment protein found in high concentrations in skeletal and cardiac muscle, functioning as an oxygen storage site ## Footnote It binds one molecule of O2 and has a higher affinity for oxygen than hemoglobin.
50
How does the oxygen dissociation curve (ODC) of myoglobin compare to hemoglobin?
The ODC for myoglobin lies to the left of the hemoglobin curve, indicating that hemoglobin can oxygenate myoglobin ## Footnote Myoglobin's curve has a hyperbolic shape, unlike hemoglobin's sigmoidal shape.
51
What adaptation occurs in Tibetan people for high altitudes?
Tibetan people possess many genes that aid in efficiently utilizing smaller amounts of oxygen ## Footnote This adaptation allows them to supply enough oxygen to their limbs while exercising at high altitudes.
52
What happens to hemoglobin's oxygen affinity at high altitudes?
At high altitude, hemoglobin's O2 affinity increases, allowing for better extraction of O2 from low-pressure areas ## Footnote This results in a left shift in the ODC.
53
What is the general properties of plasma proteins ?
• Most (>90%) synthesized in liver, • y-globulins (immunoglobulins) produced in plasma cells. • Some plasma proteins are synthesized in endothelial (von Willebrand factor) and other cells. • Most plasma proteins (all globulins) are glycoproteins. These proteins have N- and/or O-glycosidic disaccharides. • Albumin and C-reactive protein (CRP) are not glycoproteins.
54
What is the half-life plasma protein ?
Half-lives (t½) of albumin and haptoglobulin are 20 and 5 days, respectively. Blood levels of some plasma proteins (Acute Phase Proteins) rise or decrease in acute inflammatory reactions and certain types of tissue damages.