DR FATIMA ABID

ASSISTANT PROFESSOR
PHYSIOLOGY DEPARTMENT
 Total blood volume is 4.5-5 litres.

 If blood containing anticoagulants (e.g.heparin

, potassium oxalate) is centrifuged , the plasma
separates out as a supernatant while the cells
remain at the bottom.

 About 55-60% of blood is plasma

 The packed cell volume or hematocrit is about

40-45%
 Plasma is the clear straw coloured fluid
portion of the blood minus its cellular elements.

 It constitutes about 55% of the blood volume.

 Serum is plasma minus clotting factors

(fibrinogen & prothrombin ).

 The defribrinated plasma is called serum

 PLASMA contains the following composition:

WATER:
Is the main constituent of Plasma – 91%

SOLIDS:
 OTHER ORGANIC MOLECULES

Carbohydrates : Glucose ( 100-120 mg%)

Fats : neutral fats, phospholipids (150-

300mg%)

Cholesterol (150-240 mg%)

 Inorganic molecules are sodium, potassium,
calcium, magnesium, chloride, iodide, iron,
phosphates & copper.

 Gases presents in the plasma are O2 ,Co2,& N2.

plasma proteins…
- forms 7% of the solids in plasma
- their normal valves – 7.4 gm%
ranges from (6.4 – 8.3 gm%)

 INCLUDES:
ALBUMIN
GLOBULINS
FIBRINOGEN
 Total protein content of normal plasma is
6 - 8 g/100ml

 The plasma proteins consist of :

1) albumin (3.5-5 g/dl)

2) globulins (2.5-3.5 g/dl)
3) fibrinogen (200-400 mg/dl)
 The albumin : globulin ratio is usually between 1.2
:; 1 to 1.5 :1

 Almost all plasma proteins , except

immunoglobulins are synthesized in liver
 Albumin (69 kDa) is the major protein in
human plasma(3.4-4.7 g/dl)

 It makes up approximately 60% of the total

plasma protein.

 About 40% of albumin is present in the plasma,

and the other 60% is present in the extracellular
space.
 The liver produces about 12g of albumin per day ,
representing about 25% of total hepatic protein
synthesis

 Albumin can come out of vascular compartment. So

albumin is present in CSF and interstitial fluid.
 1)COLLOID OSMOTIC PRESSURE OF PLASMA:

 The total osmolality of serum is 278-305 mosmol/kg.

 This is exerted mainly by salts, which can pass easily

from intravascular to extravascular space.


 But proteins cannot easily escape out of blood
vessels, and therefore , proteins exert the
„effective osmotic pressure‟.

 It is about 25mm Hg, and 80% of it is

contributed by albumin.

 The maintenance of blood volume is dependent

on this effective osmotic pressure
 TRANSPORT FUNCTION:

 Albumin is the carrier of various hydrophobic

substances in the blood such as:

 i)bilirubin & non-esterified fatty acids

 ii)drugs (sulpha,aspirin,salicylate,)
 iii)hormones(steroid hormones,thyroxine)
 iv)metals (calcium,copper,heavy metals)
3)BUFFERING ACTION :

 Albumin has maximum buffering capacity

amongst all proteins

 It has a total of 16 histidine residues which

contribute to this buffering action.

4)NUTRITIONAL FUNCTION:

 All tissue cells can take up albumin by

pinocytosis.

 It is then broken down to amino acid level.

 So albumin may be considered as the transport
form of essential amino acids from liver to
extrahepatic cells.
1)BLOOD-BRAIN BARRIER:

 Albumin-fatty acid complex cannot cross blood-

brain barrier and hence fatty acids cannot be taken
up by brain.
2)PROTEIN-BOUND CALCIUM:

 Calcium level in blood is lowered in hypo-

albuminemia
 Thus , even though total calcium level in blood is
lowered, ionised calcium level may be normal, so
tetany may not occur.
 3) THERAPEUTIC USE:
 Human albumin is therapeutically useful to treat
burns,hemorrhage and shock.

 4)EDEMA:

 Hypo-albuminemia will result in tissue edema

 Eg: a)malnutrition
b)nephrotic syndrome
c)cirrhosis of liver
d)chronic congestive cardiac failure.
 ALBUMINURIA:
 Presence of albumin in urine is called
albuminuria.
 It is always pathological.
 Seen in:
a)Nephrotic syndrome(large quantities)
b)Acute nephritis
c)Inflammatory conditions of urinary tract.
 MICRO-ALBUMINURIA:
 In micro-albuminuria or minimal albuminuria
or plauci-albuminuria , small quantity of
albumin (30-300 mg/dl) is seen in urine

 Increased levels of microalbuminuria is an

indication of early involvement of renal tissue in
diabetic patients
 Hypoproteinemia :

 Since albumin is the major protein present in

the blood, any condition causing lowering of
albumin will lead to reduce total proteins in
blood
 HYPERALBUMINEMIA :

 Increased levels of plasma albumin are present

only in acute dehydration and have no clinical
significance
 Globulins are bigger in size than albumin .
Globulins constitute several fractions. These are:

 α1- globulin
 α2- globulin
 β- globulin
 γ- globulin
Definition:
 The Igs constitute a heterogenous family of serum
proteins, which either function as antibodies or are
chemically related to antibodies


 They constitute about 20% of all the plasma
proteins

 Igs are produced by plasma cells & to some extent

by lymphocytes
 Immunoglobulins are glycoproteins made up of
light(L) and heavy(H) polypeptide chains.

 All Igs have the same basic structure.

The basic Ig is a “Y” shaped molecule and consist of 4
polypeptide chains:

 2 H chains
 2 L chains

 The 4 chains are linked by disulfide bonds

 L chain may be either of 2 types, kappa(κ) or
lambda(λ) but not both

 The heavy chains may be of 5 types and are

designated by greek letter:
 Alpha(α)
 Gamma(γ)
 Delta(δ)
 Mu(μ)
 Epsilon(ε)
Five Classes of Immunoglobulin
 Igs are named as per their heavy chain type as IgA ,
IgG , IgD , IgM & IgE

 The L and H chains are subdivided into variable and

constant regions

 L chain consists of one variable(VL) and one

constant (CL) domain or region

 The primary function of antibodies is to protect
against infectious agents or their products.

 Igs provide resistance because they can :

 Neutralize toxins & viruses

 Opsonize microbes so they are more easily
phagocytosed
 Activate complement & prevent the attachment
of microbes to mucosal surfaces
 IgG (HEAVY CHAIN γ ) :
 Is a monomeric molecule with 2 antigen binding
sites

 There are 4 subclasses, IgG1 to IGg4 based on

antigenic differences in the H-chains and on the
number and location of disulfide bonds

 It is produced mainly in the secondary response

and constitutes an important defence against
bacteria & viruses
 IgG is the major class of immunoglobulin found in
the serum which accounts for 70% of the total

 IgG is the only antibody that crosses the placenta

& therefore is the class of maternal antibody that
protects the fetus

 Functions:
 Neutralizes bacterial toxins and viruses
 Opsonises bacteria, making them easier to
phagocytize
 Activates complements which enhances bacterial
killing
 IgA is the 2nd most abundant class constituting
about 20% of serum immunoglobulins

 IgA occurs in 2 forms:

 Secretory IgA
 Serum IgA

 Secretory IgA is a dimeric molecule



 Secretory IgA is found in external secretions

such as colostrum,saliva,tears and respiratory ,
intestinal & genital tract secretions

 Serum IgA exists as monomeric form( found in

internal secretions such as
synovial,amniotic,pleural & CSF )
 Functions:

 Secretory IgA prevents attachment of bacteria

and viruses to mucous membranes and helps
protect mucous surface from antigenic attack

 Prevents access of foreign substances to

circulation
 It is a pentamer consisting of 5 identical Ig
molecules, joined together by disulfide bridges.
 IgM accounts for some 10% of normal Ig

 IgM is the main Ig produced early in the primary

response
 As it is pentamer, it has 10 antigen binding sites &
is the most efficient Ig in agglutination,
complement activation & other antibody
reactions & is important in defence against
bacteria & viruses
 The natural blood group antibodies, anti-A &
anti-B are IgM

 IgM present on the surface of B lymphocytes is

monomer, where it functions as an antigen
binding receptor for antigen recognition

 IgM can be produced by fetus in certain

infections.

 Functions:

 Activate complement, promotes phagocytosis &

causes lysis of antigenic cells(bacteria)
 It is a monomer and resembles IgG structurally
 IgD has no known antibody function but may
function as an antigen receptor
 Like, IgM, it is present on the surface of many B
lymphocytes
 The circulating concentration of IgD in blood is
very low
 IgD is labile
 IgE is a monomeric molecule similar to IgG. It is
sometimes called reagin

 Although IgE is present in trace amounts, in

normal persons with allergic activity have greatly
increased amounts

 Functions:
 Antiallergic & antiparasitic
 IgE is responsible for anaphylactic(immediate)
type of hypersensitivity & allergy. Its main
activity is mediated by mast cells or basophils

 Defends against worm infections by causing

release of enzymes from eosinophils

 Main host defence against parasites like

helminthus, provides protection in the disease
schistomiasis