This document provides information about plasma proteins including their composition, classification, properties, functions, and changes in health and disease. It discusses that plasma is composed primarily of water but also contains proteins, organic/inorganic molecules, and gases. The major plasma proteins are albumin, globulins, and fibrinogen. Various methods can separate and analyze the different plasma protein fractions, including precipitation, electrophoresis, immunoelectrophoresis, and ultracentrifugation. The proteins have important functions such as maintaining osmotic pressure and blood viscosity, nutrient transport, blood clotting, and immune defense. Abnormalities in plasma protein levels can occur in various diseases.
2. OBJECTIVES
Plasma
Composition
serum
Plasma proteins.
Classification
Methods of separation.
Properties.
Features.
Functions.
Synthesis
Changes in health and
diseases.
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3. Plasma.
Composition.
Water (91%)
Solids. (9%)
Plasma proteins.
Organic molecules.
Inorganic molecules.
Gases.
Clear straw coloured
fluid portion of blood
minus its cellular
elements. (55%)
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4. Solids. (9%)
Plasma proteins – 7%
Normal range – 6.4-8.3gm%
Albumin, globulin, fibrinogen
& others.
Organic molecules
Carbohydrates
Fats
Non-protein nitrogenous
substances
Hormones.
Inorganic
substances – 1%
Na, K, Ca, Mg, Cl, I, Fe,
P & Cu.
Gases.
Oxygen, Co2 & N.
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5. Serum.
Blood allowed to clot
& clot retracted
remaining fluid is
serum.
So serum is plasma
without fibrinogen &
clotting factors (II,V
&VIII)
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7. Methods of separation.
Precipitation by salting out.
Cohn’s fractional
precipitation method.
Electrophoresis separation
of protein fractions.
Immunoelectrophoresis
technique.
Ultra-centrifugation
technique.
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8. Precipitation by salting out.
By sodium sulphate
solution.
By Howe (1922).
3 major fractions
Fibrinogen – removed with
clot converting plasma into
serum.
Globulins – by 22% Na2so4
Albumin –m remains in
serum.
By ammonium
sulphate solution.
Albumin precipitated
by full saturation.
Globulin – by half
saturation.
Fibrinogen by one-
fifth saturation.
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10. Cohn’s fractional precipitation
method.
Ethanol solution with
different conc. at
lower temp is used to
fractionalize plasma
proteins
Fraction I – rich in fibrinogen.
Fraction II- gamma globulins.
Fraction III – alpha & beta
globulin with isoagglutinin &
prothrombin.
Fraction IV - alpha & beta
globulin.
Fraction V – rich in albumin.
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11. Electrophoresis separation of
protein fractions.
It separate plasma proteins
into different fractions due to
electric charges of each
fractions.
Clinical use –
To know presence of abnormal
proteins
Absence of normal proteins
Change in relative conc. of
different proteins
Techniques – (FPAC)
Free boundary
electrophoresis.
Paper electrophoresis.
Agar gel
electrophoresis.
Cellulose strip
electrophoresis.
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12. Immunoelectrophoresis
technique.
It uses antigenecity &
electric charge to
separate them.
Proteins separated on
Electrophoretic
pattern by
precipitation at site of
Ag-Ab reaction.
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13. Ultra-centrifugation
technique.
Plasma proteins in
buffered solutions are
centrifuged at 60,000
rpm.
Separated due to
sedimentation
constant by property
of weight, shape &
density.
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14. Properties of plasma proteins.
Molecular weight.
Osmotic pressure.
Specific gravity.
Isoelectric point.
Electrophoretic
mobility.
Precipitation by salts.
Water solubility.
Amphoteric nature.
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15. Molecular weight.
Albumin – 69000
Globulin – 90000-
156000
Fibrinogen – 5,00,000
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18. Isoelectric point.
Can ionize either as acid
or base due to side
chain – amino group
(NH2) and carboxyl
group (-COOH).
pH at which it carries
equal positive &
negative charges is
Isoelectric point.
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20. Precipitation by salts.
This property of
proteins is utilized for
their separation by
precipitation method.
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21. Water solubility.
Due to the presence of
polar residue like NH2
& COOH they are
water soluble.
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22. Amphoteric nature.
Again due to their
presence of NH2 &
COOH groups.
They are Amphoteric in
nature.
So are efficient buffers.
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23. Features of plasma proteins.
Plasma
proteins.
Plasma
levels
Molecular
wt.
Synthesis. Half life.
Albumin 4.8 gm% 69000 Liver 10 days
Globulin. 2.3 gm % 90000-
156000
Liver
Fibrinogen. 0.3 gm% 400000-
500000
Liver
Prothrombin
.
40 mg% 68000 Liver
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24. Different forms of Globulins.
Ceruloplasmin.
Fetunin.
Glycoprotein.
Haptoglobulin.
Angiotensinogen.
Transferrine.
Immunoglobulin.
Lipoproteins.
Haemagglutinins.
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25. Functions of Plasma Proteins.
Suspension stability of
blood.
Fibrinolytic function.
Osmotic pressure.
Blood viscosity.
Coagulation of blood.
Defense mechanism of
body.
Transport function.
Reserve proteins.
Acid base balance of
the body.
Nourishment of tissue
cells.
Genetic information
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26. Suspension stability of blood.
It’s the property of
RBC due to which they
remain suspended.
Globulin & fibrinogen
– mainly responsible.
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27. Fibrinolytic function.
Digest intravascular
clot ( Thrombus)
Save from
intravascular
thrombosis.
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28. Osmotic pressure.
Mainly proteins can't
pass through capillary
membrane so exert
osmotic pressure.
About 25 mmHg.
70-80% due to
albumin.
Imp for exchange of
fluids.
At Arterial end
At Venous end.
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29. Blood viscosity.
Due to size & shape of
plasma proteins.
Mainly fibrinogen &
globulins due to its
asymmetrical shape.
viscosity
resistance
Blood pressure.
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30. Coagulation of blood.
Mainly fibrinogen,
Prothrombin and other
coagulation proteins.
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31. Defense mechanism of body.
Mainly gamma
globulins against
microorganisms.
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32. Transport function.
Sr no COMOUND TRANSPORTER
1 CO2 AS CARBAMONO COMPOUND
2 THYROXINE THYROXINE BINDING PROTEIN.
3 CORTISOL TRANSCORTIN.
4 VIT A,D,E HDL,LDL
5 BILIRUBIN ALBUMIN
6 VIT B12 TRANSCOBALAMINE
7 DRUGS ALBUMIN
8 COPPER CERULOPLASMIN
9 FREE HAEMOGLOBIN HAPTAGLOBIN
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33. Reserve proteins.
Utilized by body tissue
during conditions like
Fasting
Inadequate protein
intake
Excessive catabolism of
body proteins.
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34. Acid base balance of the body.
Contribute 15% of
total buffering
capacity of blood.
In acidic pH NH2 acts
as base & accepts
proton
In basic pH – COOH
acts as acid & donate
proton.
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35. Nourishment of tissue cells.
Plasma proteins used
by WBC to produce
substances known as
Trephones or Carrel.
Essential for
nourishment of tissue
cells.
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36. Genetic information
Plasma proteins exhibit
polymorphism.
It’s a Mendelian Trait.
Valuable tool for
population genetics study.
Mainly haptoglobin,
immunoglobulin,
ceruloplasmin &
transferrin.
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37. Synthesis of plasma proteins.
Site.
In embryo – Mesenchymal cells.
In Adult –
Albumin & Fibrinogen by retculoendothelia cells of liver.
Alpha & beta globulins by liver, spleen & bone marrow.
Gamma by B Lymphocytes.
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38. Factors affecting Synthesis of
plasma proteins.
Dietary proteins.
Relationship between dietary proteins & plasma
proteins is studied by “Whipple” by experiment
called “Plasmapheresis”.
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39. Plasmapheresis.
Dog made
hypoproteinemic by
repeatedly withdrawing
blood & reinjecting
cellular elements.(in
Ringer Locke RL) till
protein 4gm/100ml.
Then different standard
diets are given
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40. Conclusions.
Dietary proteins – essential.
Chemical resemblance – determine efficacy.
Essential amino acids – must for synthesis.
Dietary proteins of animal origin – favors
albumin synthesis.
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41. Conclusions.(cont….)
Dietary proteins of plant origin - Globulin
synthesis.
Regeneration period – 14 days.
Rate of regeneration – very fast within first 24
hrs.
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42. Other factors.
Presence of infection. –
reduces plasma protein
synthesis.
Exposure to antigen –
stimulate formation of
antibodies.
Inflammatory
conditions – promotes.
Colloid oncotic pressure
affects albumin synthesis.
Interleukin I by
activated
macrophages
stimulate synthesis.
Prostaglandins –
increases acute phase
proteins.
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43. Changes in plasma proteins in
health & disease.
Normal levels.
Total Proteins – 7.4gm%
Albumin – 4.8 gm%
Globulin – 2.3 gm%
Albumin/globulin ratio. – 1.7:1
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47. Reversal of normal A:G ratio.
Normal ratio 1.7:1
Reversed in
Liver diseases as albumin synthesis decreases.
Hypoproteinemia as globulin levels increases.
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