1. Plasma protein
and their clinical
significance and
dysproteinemia
PRESENTED BY- MOHAMMED IRFAN
ID/NUMBER- TV/2022-41
GUIDED BY: DR. T. V. CHAITANYA
KUMAR
COLLEGE OF VETERINARY SCIENCE TIRUPATI
DEPARTMENT OF VETERINARY BIOCHEMISTRY
2. Plasma protein consist of
water electrolytes nutrient
protein and hormone
The total concentration of
plasma protein is about 6-
8 g/dl
The plasma protein are
complex mixture that
include not only simple
protein but also
conjugated protein such
as glycoprotein and
lipoprotein
Plasma protein - introduction
4. Separation of plasma protein
There are two
methods of plasma
protein separation
Salting out method :
separation of three
major group of
protein like
albumin, globulin
and fibrinogen
By using of various
concentration of
sodium and
ammonium sulfate
Electrophorosis :
separation of plasma
protein into five
distinct band
Albumin , alfa –1 or
alfa-2 globulin, beta
or gama globulin
5. Albumin
• It is major constituent
(60%) of plasma
protein
• The concentration of
albumin is 3.5 to 5 g/dl
• The half life of
albumin is 20 days
• Normal A/G ratio is 1.2
to 1.5
6. Function
of
albumin
Osmotic
function: it is
responsible for
75 to 80% of
osmotic
pressure of
plasma due to
low molecular
weight
Transport
function: like
free fatty acid
bilirubin , calciu
m and copper
Nutritive
function: it is
serve as source
of amino acid
for tissue
protein
synthesis
Buffering
function: it has
a maximum
buffering
capacity
7. Synthesis
and
structure
of
albumin
The liver produce about 12 g of
albumin per day
Which represents about 25% of
hepatic protein synthesis
Molecular weight is 69kDa
It is a small polypeptide chain of
585 amino acid with 17 disulfide
bond
8. Clinical
significanc
e of
albumin
• Blood brain barrier: albumin binds to
certain compond in plasma prevent
them from crossing the BBB
• Ex: albumin –bilirubin complex
• Hypoalbuminemia: low level of plasma
albumin(<2g/dl) seen in
• Cirrhosis of liver
• Malnutrition
• Nephrotic syndrome
• Albuminuria
• Drug interactions
9. Globulin
• Its concentration in
plasma is 2.5 to 3.5g/dl
• It is bigger in size
compare to albumin
• There are four type of
globulin
• Alfa-1 globulin
• Alfa-2 globulin
• Beta globulin
• Gamma globulin
10. Synthesis and structure of globulin
• Molecular weight range from
90 to 130 kDa
• Alfa or beta globulins are
synthesize in liver
• Gamma globulin is synthesized
in plasma cell and B-cell of
lymphoid tissue
11. Alfa –1 globulin(alfa-1 antitrypsin)
•Also called alfa-1 antiprotease
•It is glycoprotein with 394AA and molecular weight 54kDa
•It is protease inhibitor
•Function: It is combines with trypsin
• elastase to inhibit their activity
•Clinical significance
•Emphysema – abnormal distension of lungs by air
•Liver cirrhosis - accumulation of mutant alfa1 AT which forms polymers
•Then it is cause hepatitis followed by accumulation of collagen
13. Alfa –2 globulin- clinically importance
• Alfa-2 macroglobulin
• Its conc in plasma is elevated in
nephrotic syndrome
• Clinical significance- due to low
molecular wt protein are lost in
urine (proteinuria)
• Haptoglobulin
• It is glycoprotein and acute phase
protein
• Function- it is formed haptoglobin
hemoglobin complex
• It cannot pass through
glomeruli of kidney while
hemoglobin is free
• Clinical significance- decrease
hemolytic animia
• Ceruloplasmin
• It is blue colour copper
containing protein
• Its bind 90% of plasma copper
• Its posses oxidase activity and
associated with wilson disease
15. Beta globulin -
types and clincal
imprtance
• Transferrin- it is glycoprotein
• It is associated with beta globulin
• It is transporter of iron in circulation
• C-reactive protein (CRP)
• It is major component of acute phase
protein
• It is produced by liver
• Increase level of high sensitive CRP in
circulation are useful for predicting risk of
Coronary heart disease
16. Gamma
globulin
• Immunoglobulin is a functional term and
gamma globulin is physical term
• It is separated by elecrophorosis
• Structure and synthesis
• It is Y shaped tetramer
• All immunoglobulin consist heavy and light
chains
• Its held together by disulfide bond and non
covalent interaction
• Each heavy chain is made by 450 amino
acid
• Each light chain is made by 212 amino acid
20. Dysproteine
mia
It is a medical condition characterized by an abnormal level of
protein composition in blood
Main types of dysproteinemia
Hyperproteinemia – excess protein in blood
Hypoproteinemia- low protein level of blood
Dysglobulinemia- abnormal globulin level
Paraproteinemia- presence of abnormal proteins
Monoclonal gammopathy- abnormal antibody production
Polyglobulinemia- excess globulin in blood
21. Dysproteine
mia can be
caused by
various
factors
Genetic
mutations
Inflammator
y response
Immune
system
disorder
Cancer
(multiple
myeloma)
Infections
Liver or
kidney
disease
