PLASMA PROTEIN

Introduction
The plasma proteins are:
1. Serum albumin
2. Serum globulin
3. Fibrinogen.
The serum (chapter 7) contains only albumin and globulin. The fibrinogen is absent in
serum because of in converted into fibrin during blood clotting. Because of this, the
albumin and globulin are usually called serum albumin and serum globulin.

NORMAL VALUES

The normal values of the plasma proteins are:

Total proteins : 7.3g/dL (6.4-8.3g/dl)
Serum albumin : 4.7g/dL
Serum globulin : 2.3g/dL
Fibrinogen : 0.3g/dL

SEPARATION OF PLASMA PROTEINS

His plasma proteins are separated by the following methods:

1. PRECIPITATION METHOD
Proteins in the serum are separated into albumin and globulin. This is done by
precipitating globulin with 22% sodium sulfate solution.The albumin remains in
solution.

2. SALTING OUT METHOD

SERUM GLOBULIN IS SEPARATED INTO TWO FRACTIONS
CALLEDEUGLOBULIN AND PSEUDOGLOBULIN BY SALTING OUT
WITHDIFFERENTSOLUTIONS.

3. ELECTROPHORETIC METHOD
In this the plasma proteins are separated depending their differences in electrical
charge and the rate of migration.

4. CHON’S FRACTIONAL PRECIPITATIONMETHOD

By this method, plasmaproteins are separated into albumin and different fraction of
globulin depending upon their solubility.
5. ULTRACENTRIFUGATION METHOD
In this method albumin, globulin and fibrinogen re sepa-rated depending upon their
density. This method is also useful in determining the molecular weight of these
proteins.

6. GEL FILTRTION CHROMATOGRAPHY

It is a column chromatographic method by which the proteins are separated n the
basis of size.

7. IMMUNOELECTROPHORETIC METHOD
By this method the proteins are separated on the basis of electrophoresis patterns
formed by precipitation at the site of antigen antibody reactions.

PROPERTIES OF PLASMA PROTEINS

1. MOLECULAR WEIGHT
ALBUMIN : 69,000
Globulin : 1, 56,000
Fibrinogen : 4, 00,000

2. ONCOTIC PRESSURE
The plasma proteins are responsible for the entotic or osmotic pressure in the blood.
The osmotic pressure exerted by proteins in the plasma is called colloidal about
25mmHg. Albumin plays a major role in exerting oncotic pressure.

3. SPECIFIC GRAVITY
The specific gravity of the plasma proteinsis 1.026.

4. BUFFER ACTION
The acceptance of hydrogen ions is called buffer action. The plasma proteins have1/6
of total buffering action of the blood.

FUNCTIONS OF PLASMA PROTEINS

1. ROLE IN COAGULATION OF BLOOD

Fibrinogen is essential for the body.

2. ROLE INDEFENSE MECHANISM OF BODY

The gamma globulins play an important role in the defense mechanism of the body by
acting as antibodies. These proteins are also called immune-globulins.
3. ROLE IN TRANSPORT MECHANISM
The alpha and beta globulins play an important role in the transport of metals in the
blood
.
4. ROLE IN MAINTENANCE OF OSMOTIC PRESSURE IN BLOOD
At the capillary levell.most of the substance are exchanged between the blood and the
tissues

5. ROLE IN REGULATION OF ACID-BASE BALANCE

Plasma proteins particularly the albumin plays an important role in regulating the
acid-base balance in the blood.

6. ROLE IN VISCOSITY OF BLOOD

The plasma proteins provide viscosity to the blood which is important to maintain the
blood pressure.

7. ROLE IN ERYTHROCYTE SEDIMENTATION RATE (ESR)

Globulin and fibrinogen accelerate the tendency of rouleaux formation by the red
blood cells.

8. ROLE IN SUSPENSION STABILITY OF RED BLOOD CELLS

During circulation, the red blood cells remain suspended uniformly in the blood. This
property of the red blood cells is called the suspension stability.

9. ROLE IN PRODUCATION OF TREPHONE

Trephine substances are necessary of nourishment of tissue cells in culture .These
substance are produced by leukocytes from the plasma proteins.

10. ROLE AS RESERVE PROTEINS

During fasting inadequate food intake or inadequate protein intake the plasma
proteins are utilized by the body tissues as the last source of energy.

BIBLIOGRAPHY:-
1. Text Book of physiology, A.K. Jain
2. Essentials Book of medical physiology, K. Sembulingam
 AMINO ACID POOL

INTRODUCTION:-
An adult has about 100g of free amino acids which represent the amino pool of the body.
Glutamate and glutamine together constitute about50% and essential amino acids about
10% of the body pool (100g) the concentration of intracellular amino acids is always
higher than the extra cellular amino acids. The amino acid pool of body is maintained by
the sources that contribute input and the metabolic pathways the utilize output the amino
acids.

1. Sources of amino acid pool

Turnover of body protein intake of dietary protein and the synthesis of non-essential
amino acid contribute to the body amino acid pool.

A. Protein turnover:
The protein present in the body is in a dynamic state .it is estimated that about 300-
400g of protein per day is constantly degraded and synthesized which provide body
turnover.

B. Direct protein
There is a regular lose of nitrogen from the body due to degradation of amino
acids .in healthy adults ,it is estimated about that (30-50g/day) must therefore be
supplied in the diet to manage nitrogen balance .the purpose of directory protein is to
supply amino acids particularly the essential ones for the synthesis of proteins and
other nitrogen compounds

C. Synthesis of nonessential amino acids :

Ten out of the 20 contribute naturally occurring amino acids can be synthesized by
the body which the amino acids
2. Utilization of amino acid pool from body pool

A Most of the body proteins 300-400g/day degraded are synthesized from the amino
acids pool .these include enzymes, hormones immunoproteins contractile proteins etc.

B. many important nitrogenous compounds porphyries etc are produced from the amino
acids .about 30g of the protein is utilized for this purpose.

C Generally about 10-15% of body energy requirements are met from the amino acids

D The amino acids are converted to carbohydrates and fats this become s predominant
when the proteins consumption is in the body requirements.
BIBLIOGRAPHY:-
1.U.Satyanaryana
2.

THE ELBOW JOINT

The elbow joint is a synovial joint between the lower end of hummers and the upper ends
of the radius and ulna bones.

Surface Marking
The joint line is situated 2cm below the line joining the two epicondyles and slopes
downwards and medially. This slope is responsible for the carrying angle

Articular surface
Upper: The capitula and trohlea of the hummers.

Lower: 1 upper surface of the radius articulates with the capitula, (ii) trochlear notch of
the ulna articulates with the trochee of the hummers.

The elbow joint is contionuous with the superior radioulnar join. The humeroradial,the
humeroulnar and the superior radioulnar joints are together known as cubical
Ligaments

1. Capsular ligament superiorly, it is attached to the lower end of the hummers in such a
way that the captulum.
2. The anterior ligament
3. The posterior ligament
4. The ulnar collateral ligament
5. The radial collateral or lateral ligament

Relations of Elbow joint

Anteriorly: Brachialis, median nerve, brachial artery and tendon of biceps.

Posteriorly: Triceps
Medially: Ulnar Nerve
Laterally: Supinator extensor carpi radialis brevis

Blood Supply

From anatomists around the elbow joint.

Nerve Supply

i. Ulnar nerve,
ii. median nerve,
iii. radial nerve
iv. musculocutaneous nerve

Movements

1. Flexion- the Brachialis,the biceps, the brachioradialis

2. Extension-The triceps, the ancones