Unit 2-Lecture 1-Antibodies

Unit 1-Lecture 4
Chapter 2
ANTIBODY
Contemporary Clinical Immunology and Serology

Kate Rittenhouse-Olson | Ernesto De Nardin
Why Are Antibodies Important?
 Key in helping us fight infection
 Vital to many diagnostic tests
 Diagnose infection, autoimmunity,
allergy
 To find an antigen in the patient for:
 infectious disease testing
 cancer diagnosis
 pregnancy testing
 drug testing
 therapeutic drug concentration testing
Why Are Antibodies
Important?
 Biotechnology industry
 Utilized in research and in the
biotechnology industry

Immunoglobulins(Antibody)
 Proteins that bind to antigen in a “lock
and key” fashion
 Each antigen stimulates production of
specific antibody such as a specific key fits
into a specific lock.

Serology
 The study of the reaction and
properties of the serum components
of the blood
 Deals mostly with antibody and antigen
reactions in vitro

Immunoglobulins
(Antibody)
 Theories of antibody diversity
 Early 1900’s –postulated that antigens selected
cells with the built in capacity to respond to it.
 1930’s – Antibody producing cells thought to be
capable of synthesizing a generalized type of
antibody
 Antigen contact prompted protein alteration resulting
in specific antibody production
 Antigen served as a mold or template

Immunoglobulins
(Antibody)
 Theories of antibody diversity
 1960’s – the description of the antibody was
accepted
 Antibodies were described as having a constant region
and a variable region coded by separate genes
 Gene recombination provides the ability for specificity to an
antigen

Antibody Structure and Function
 Immunoglobulins
 Glycoproteins found in the serum portion of the
blood.
 Composition
 82–96 percent polypeptide
 2–14 percent carbohydrate.

 Considered to be the humoral branch of the
immune response.
 Produced in response to antigenic stimulation
 Produced by B-cells/plasma cells
 The use of antigen to detect antibodies or the
use of antibody to detect antigen has been the
basis of serological testing in the laboratory
for years.

 Immunoglobulins Exist in TWO forms
1. Membrane bound on B-cell surface
 Act as receptors
2. Secreted by plasma cells and may reside in
circulation, tissues, and mucosal sites
 Binds to antigen
 Neutralizes toxins
 Prevents entry and/or spread of pathogens
 May also attach to surfaces of other effector cells
 i.e. Neutrophils, macrophages, NK cells, mast cells

 All immunoglobulin molecules are made up of a basic
four-chain polypeptide unit
 Two large chains called heavy
 H chains
 Gives antibody its name
 Two smaller chains called light
 L chains.
 Both Kappa or both Lambda
 These two pieces occur in equal amounts
 H2L2
 These chains are held together by noncovalent forces
and disulfide interchain bridges.
Structure of Immunoglobulin Molecule
 Fab (fragment antibody)
 Contains the antigen-binding site
 Contains the variable region
 Weight of approximately 45 kD each
 Fc (fragment crystallizable)
 Contains the constant region
 Weight of approximately 50 kD each

General Structure

Serum Protein
Electrophoresis

General Structure
 Two dissociating chemicals used to
determine IgG structure
 Urea and mercaptoethanol
 Two enzymes also used
 Papain
 Fragment crystallizable (Fc)
 Fragment antigen binding (Fab)
 Pepsin
 1 dimeric F(ab)’2
 Two small fragments of the Fc area

Antibody Structure

General Structure-Urea &
Mercaptoethanol.

General Structure-Papain

Cleavage of Antibody Molecule
with Papain

General Structure-Pepsin

Cleavage of Antibody Molecule
with Pepsin

General Structure
 Antigen binding site
 The N-terminal end of the heavy chain
and the light chain
 Called the paratope
 The part of the antigen that the
antibody binds
 Called the epitope
 Bound by noncovalent bonds
 Van der Waals bonds, hydrogen bonding,
electrostatic or ionic bonds, and hydrophobic and
hydrophilic interactions
General Structure
 Binding
 Affinity
 The sum of the attractive interaction
between the paratope and the epitope
 Avidity
 The sum of the binding of all the paratopes
and the epitopes
 Ex: in IgG Avidity = 2 times affinity

Heavy and Light Chains
Each monomer of antibody (ab) contains:
 2 identical heavy chains – gives antibody class name
 mu (IgM), delta (IgD), gamma (IgG), alpha (IgA), epsilon
(IgE)
 2 identical light chains
 kappa or lambda
 Light chains in each molecule are both kappa or both lambda,
never 1 of each
 Heavy and light chains connected by disulfide bonds
 L-chains bonded to the H-chains by S-S bonds
 H-chains joined to each other by 1 or more disulfide bonds
 the exact number of bonds differs with the class and subclasses.
Nature of Light Chains
 Each light chain sequence contains between 200-220
amino acids
 Variable region – sequence 1-110
 1 is the terminal position
 Constant region – sequence 111- 200 or 220
 Difference between κ and λ chains
 Amino acids substitutions at a few locations along the chain
 No functional differences
 Both κ and λ found on all five classes of Ig, but only one type is
present in a given molecule

The Hinge Region
 The segment of H chain located between the CH1

and CH2 regions is known as the hinge region.
 It has a high content of proline and hydrophobic residues
 the high proline content allows for flexibility.
 This ability to bend lets the two antigen-binding sites
operate independently.
 The flexibility also assists in effector functions
 initiation of the complement cascade
 Gamma, delta, and alpha chains all have a hinge
region, but mu and epsilon chains do not.
 However, the CH2 domains of these latter two chains are
paired in such a way as to confer flexibility to the Fab arms.

General Structure
 Variable regions of heavy and light
chains
 Different binding abilities due to
hypervariable regions
 3 in the VL, 3 in the VH
 Also called Complementary Determining
Regions (CDRs)
 Shape is complementary to antigen shape
 Framework regions
 Stretches in the variable domains between
hypervariable regions
General Structure
 Structural studies of immunoglobulin
 Aided by the use of myeloma proteins
 Identical immunoglobulin molecules
produced by a clone of tumor cells
 Myeloma cells that are plasma cells
 These immunoglobulins are identical
 Identical Fab
 Identical Fc regions
 Natural type of monoclonal antibody

 Immunoglobulin (Ig) Classes
 IgG(γ) – major immunoglobulin in blood
 4 subclasses
 IgM(μ) – largest; effective in microbial killing
 IgA(α) – secretory; present in body fluids
 2 subclasses
 IgE(ε) – seen in allergy and parasitic infections
 IgD(δ) – regulates activation of B cells
 All classes of immunoglobulins share the same
basic structural characteristics
Immunoglobulin Class

Immunoglobulin Class

Classes, Subclasses, and
Light Chains
 The different classes
 The FAB region
 Composed of heavy and light chains
 Differences in the heavy chains lead to
their different biologic functions
 The Fc region
 Made up of only parts of the heavy chain
 The difference in biological activity is due to
heavy chain differences in the Fc region

Antibody Structure and Function-IgG
 IgG – 2γ H-chains 2L-chains

 The predominant immunoglobulin in
humans,
 80 % of the total serum immunoglobulins.
 Only Ig capable of crossing the placenta
 IgG has the longest half-life of any
immunoglobulin class,
 Approximately 23–25 days
 May help to account for its predominance in serum.
 Major functions
1. Providing immunity for the newborn
 IgG can cross the placenta;
2. Activates classical complement pathway
3. Acts as an Opsonin
4. Neutralizes toxins and viruses
1. Usually by blocking binding
5. Participation in agglutination and precipitation reactions.
6. Responsible for long-term immunity
 Antibody produced in amenestic response

 There are four major subclasses,

 IgG1 - 67 percent
 IgG4 - 4 percent.
 These subclasses differ mainly in the number
and position of the disulfide bridges between
the γ chains.
 IgG3
 Has the largest hinge region and the largest number of
interchain disulfide bonds
 It is the most efficient at binding complement, followed
by IgG1.
 IgG2 and IgG4 have shorter hinge segments
 Tends to make them poor mediators of complement
activation.
 IgG1 and IgG3 are best at opsonization.
 All subclasses of IgG appear to be able to cross the
placenta
 IgG2 is the least efficient.

IgG Subclasses
Subclass Placental Complement Opsonic Half-Life

Transfer Activation
IgG1 + + ++ 23
IgG2 +/- +/- +/- 23
IgG3 + + ++ 8
IgG4 + - + 23

General Structure

Antibody Structure and Function-IgM
 2μ H-chains, 2L-chains
 Macroglobulin
 Molecular weight of approximately 970,000 d.
 5–10 percent of all serum immunoglobulins.
 Found mainly in the intravascular pool and not in other body fluids or tissues
 Because of its large size
 Half-life – about 10 days
 much shorter than that of IgG.
 Presence classifies B-cell as being mature
 It is synthesized only as long as antigen remains present,
 No memory cells for IgM.
 Does not cross the placenta
 IgM can exist as a monomer or as a pentamer.
 The pentamer form is found in secretions
 The monomer form occurs on the surface of B cells.

 IgM Pentamer Form
 The five monomeric units are held
together by a J, or joining, chain
 Glycoprotein with several cysteine residues.
 These serve as linkage points for disulfide bonds
between two adjacent monomers.
 IgM configured as a pentamer assumes
a starlike shape with ten functional
binding sites
 only about five of these are used unless the
antigen is extremely small.
Light Chains
 IgM-Monomer form
 On surface of B cells
 Receptor for specific antigen
 Monomeric not pentameric
 Slightly different Fc region
 Transmembrane and cytoplasmic regions

IgM

 IgM Functions
1. Primary response antibody
 It is the first to appear after antigenic stimulation
 The first to appear in the maturing infant.
2. Effective activator of classical complement pathway
 Due to size
3. Agglutination
4. Opsonization
5. Neutralization of toxins
6. Surface receptors for antigens

 The following slide depicts the difference between
the primary response and the secondary response.
 The primary response
 predominantly IgM
 Characterized by a long lag phase
 The secondary response
 Predominately IgG
 Has a shortened lag period and a much more rapid increase in
antibody titer.

IgM

IgM

IgM

Antibody Structure and Function-IgA
 IgA – 2α H-chains 2L-chains
 10–15 percent of all circulating immunoglobulin.
 Synthesized in plasma cells found primarily in
MALT
 Synthesized at a rate 2x that of IgG
 Two subclasses of IgA
1. IgA1 -usually a monomer primarily found in serum
2. IgA2 – dimer or tetramer with a Secretory Component

 IgA Functions
1. Patrols mucosal surfaces and act as a first line of
defense
2. Neutralizes toxins produced by microorganisms
3. Helps to prevent bacterial adherence to mucosal
surfaces.
4. Act as Opsonins
5. Phagocytosis promoter
6. Aggregation of IgA immune complexes may
trigger the alternate complement pathway
 Not capable of fixing complement by the
classical pathway
Light Chains
 IgA
 Specific Secretory functions
 Prevents the entrance of pathogens
 Cross-links multiple epitopes to form
aggregates
 Easily removed by the ciliated cells of the
mucous membranes and by gut peristalsis
 Also functions by blocking adhesion of the
bacteria, virus, or toxin

IgA
 Transferred through breast milk
 Does not cross placenta
 One of breast milks most important
proteins
 ~90% of immunoglobulins found in breast
milk or colostrum

Light Chains
 IgA Subclasses
 IgA1
 Main component of serum IgA
 Molecular weight – ~160,000
 Consists of about 472 amino acids.
 IgA2
 ~445,000 daltons
 Main component of secreted IgA
 Made by 4 genes and 2 cells

Figure 2.6
(a) IgA. (b) IgA production.

 IgD – 2δ H-chains 2L –chains

 Discovered in1965, when it was found in a patient
with multiple myeloma.
 Synthesized in low levels
 Only ~ 0.2% of serum immunoglobulin
 Molecular weight - approximately 180,000.
 The δH chain has a molecular weight of 62,000

IgD
 Appears to have an extended hinge region
 Consisting of 58 amino acids.
 More susceptible to proteolysis than other
immunoglobulins due to this long hinge
region
 Short half-life of 2 to 3 days most likely due to
this

 IgD Functions
 No definitive functions, but thought to stimulate
proliferation of B-cells or stimulation of T-cells
 Most of the IgD present is found on the
surface of immunocompetent but unstimulated
B lymphocytes.
 It is the second type of immunoglobulin to
appear (IgM being the first)
 The high level of surface expression and its
intrinsic flexibility make it an ideal early
responder to antigen.
 B lymphocytes bearing only IgM receptors
appear incapable of an IgG response.
 Those with both IgM and IgD receptors are
capable of responding to T-cell help and
switching to synthesis of IgG, IgA, or IgE.
 IgD may thus play a role in regulating B-cell
maturation and differentiation.

IgD

 IgE – 2ε H-chains 2L-chains
 The least abundant immunoglobulin in the serum
 0.0005 percent of total serum immunoglobulins.
 The ε H chain is composed of around 550 amino acids
distributed over one variable and four constant domains.
 ~ 190,000 daltons due to extra CH region which binds mast
cells
 The plasma cells that produce IgE
 Located primarily in the respiratory tract and skin.
 Does not participate in typical immunoglobulin reactions such
as complement fixation, agglutination, or opsonization.
 Cannot cross the placenta.

Light Chains
 IgE
 Dramatic effects
 Responsible for immediate type
hypersensitivity
 Important protective role
 Responds to pathogens that have penetrated
IgA response
 Triggers inflammatory response
 Brings eosinophils and neutrophils to area

Light Chains
 IgE
 Binds to mast cells
 Binding of the antigen will cause mast cell
degranulation
 Releases histamine, heparin, and chemotactic
factors
 Substances cause the classic symptoms of
allergy, hay fever, asthma, vomiting,
diarrhea, hives, shock, and anaphylactic
death

IgE

IgE

Light Chains
 IgE
 Protective role for things that have
penetrated the mucosa, such as
parasites
 Triggers inflammatory response
 Brings eosinophils, neutrophils to the area

Light Chains
 Vaccination of an animal with
human immunoglobulin
 Produces antibodies to different regions
of the immunoglobulins
 Isotypic determinants
 Allotypic determinants
 Epitope
 Called idiotype
 May regulate immune response


Diversity
 The Side-chain theory

 One of the first theories to be formulated in an attempt to
explain antibody diversity was that of Paul Ehrlich in the
early 1900s.
 Ehrlich postulated that certain cells had specific surface receptors
for antigen that were present before contact with antigen occurred.
 Once antigen was introduced, it would select the cell with the
proper receptors, combination would take place, and then receptors
would break off and enter the circulation as antibody molecules.
 It was further postulated that this process could be repeated upon further contact
with antigens.

Diversity
 The receptors Ehrlich originally postulated are in fact
the surface immunoglobulins IgM and IgD, found
on immune-competent but unstimulated B
lymphocytes.
 Repeated contact with antigen would continually increase a
specific lymphocyte pool.
 Such a model provides an explanation for the kinetics of the
immune response.
 Ehrlich’s side-chain theory laid the foundation for
further hypotheses.
Diversity
 Clonal selection theory
 Proposes how the huge and diverse
immunoglobulin repertoire could exist
 Key idea:
 lymphocytes that can only react with one
antigen, before any encounter with antigen has
occurred
 When these lymphocytes interact with antigen they
proliferate and make a clone of cells that respond only
to that antigen

Diversity
 Conservation of DNA
 Antigen-independent
 Random recombinational events of DNA
gene segments during B-cell maturation
 Antigen-dependent
 Clonal deletion of self-reactive B cells
 Antigen-dependent
 Somatic mutation and affinity maturation

Diversity
 In 1965, Dryer and Bennett proposed a solution to the
issue of the large number of genes required by the
clonal selection theory.
 They suggested that the constant and variable portions of
immunoglobulin chains are actually coded for by separate
genes.
 There could be a small number coding for the constant region
and a larger number coding for the variable region.
 This would considerably simplify the task of coding for such
variability of antigens.
 Scientific evidence now indicates that this is exactly
what happens, through genetic rearrangements within
the lymphocytes.

Antigen-Independent
Diversity
 Random recombinational events of
DNA gene segments during B-cell
maturation
 Heavy chain variable regions
 Encoded by three gene segments
 V, D, and J genes
 Gene segments after recombination are
joined to the heavy chain constant region

Antigen-Independent
Diversity
 Light chain variable region
 Encoded by two gene segments
 V and J genes
 Gene segments are joined to the light
chain constant region after a
recombinational event

Antigen-Independent Diversity
 Tonegawa discovery
 Human immunoglobulin heavy chains
 Made by genes from chromosome 14
 Human immunoglobulin kappa light chains
 Human immunoglobulin lambda light
chains

Diversity of the Immunoglobulin Molecule
 Diversity – the key to adaptive humoral IR
 B cells recognize and respond to many different foreign
epitopes
 Essential for combating bacteria and fungi
 Key to vaccination against bacteria and virus
 Germline DNA for variable regions of heavy and light chains
rearranged before transcription
 If successful – B cell matures further
 Mu chains present
 If unsuccessful – B cell dies by apoptosis

Antigen-Independent
Diversity
 The multiple binding sites in the
variable region produced prior to
interaction with the antigen
 The result of random recombination
 For the heavy chain of
 Over 50 different VH gene segments
 27 functional D gene segments
 6 J gene segments

Antigen-Independent
Diversity
 The multiple binding sites in the
variable region produced prior to
interaction with the antigen
 The result of random recombination
 For the light chain of about 40 Vk gene
segments and 5 Jk gene segments
 For the kappa C region, segment of 30 Vl gene
segments and 4 Jl gene segments for the 4
lambda light chain C region gene segments

Antigen-Independent
Diversity
 Genetic rearrangement must occur for
functional immunoglobulin to be made
 Constant regions
 Order: μ, δ, γ3, γ1, α1, γ2, γ4, α2, and ε for
the heavy chain class types
 Initially, each B cell that produces
immunoglobulin rearranges the VDJ with the
μ constant region for the initial production
of IgM
Antigen-Independent
Diversity
 Antibody diversity method
 DNA manipulation occurs to get V, D,
and J segments together
 Nonamers or heptamers
 Bind complementary heptamer or nonamer
 The joining process
 Has some built-in variability
 Slight changes in where the junction occurs

Antigen-Independent
Diversity
 Antibody diversity method
 Nonamers or heptamers
 The joining process
 Addition or deletion of nucleotides, which can
result in a different binding site
 Combining all these things antigen-independent
diversity can encode for tens of millions of
different specificities

Antigen-Dependent Clonal
Deletion
 Decreases diversity in a mechanism
 Helps maintain the self–non-self
recognition system of the acquired
immune response
 Maturational arrest occurs
 Occurs if a maturing B cell meets and
binds with its antigen prior to maturation
 Does not become a mature B cell

Antigen-Dependent Clonal
Deletion
 Apoptosis
 A process by which the B cell, after
receiving certain signals, produces
enzymes that degrade its own DNA to
commit cellular suicide

Antigen-Dependent Somatic
Mutation and Affinity Maturation
 The final process in the antibody
repertoire development
 Antigen dependent somatic mutation
and affinity maturation

Antigen-Dependent Somatic Mutation
and Affinity Maturation
 When a B or T-cell binds antigen

 Rapid proliferation of the cell occurs
 Initially each offspring cell is identical in
binding to the original parental cell
 Mutation occurs during this rapid
proliferation
 Cells that have increased affinity of
binding are selected and proliferate
more
Class Switching, Cont.
“Looping out” of intervening DNA to produce VDJ-C 1.

Class Switching, Cont.
Class switching. In this example, DNA is “looped out” during recombination of switch regions Sµ and Sa to
obtain DNA with a combined SµSa and permanent removal of DNA containing the Cµ, Cd, Cg, and Ce genes. This
leads to the production of DNA having the same variable VDJ and producing IgA rather than IgM.

Heavy Chain Class Switching
 First immunoglobulin made is IgM
 Downstream of the  gene segment are
gene segments for all the other heavy
chain types
 T cell help guides class switching
 Secretion of cytokines that cause the B cell
to excise the m gene segment
 One cell-one specificity rule ,different heavy
chain type, while its binding site remains
the same

Monoclonal Antibodies
 Myeloma proteins
 Discovery has facilitated studies on
immunoglobulin
 Monoclonal antibodies are prepared
intentionally, usually using a mouse
 Consistent source of antibody of a
defined specificity and sensitivity
 Utilized in clinical assays to identify
antigens
 The knowledge that B cells are genetically preprogrammed to
synthesize very specific antibody has been used in developing
antibodies, known as monoclonal antibodies, for diagnostic
testing and for therapeutic purposes.
 Normally, the response to antigen is heterogeneous, because
even a purified antigen has multiple epitopes that stimulate a
variety of B-cell clones.
 In 1975, Georges Kohler and Cesar Milstein discovered a
technique to produce antibody arising from a single B cell,
which has revolutionized serological testing.

 Kohler and Milstein’s technique
 Fuses an activated B cell with a myeloma cell (a cancerous
plasma cell line) that can be grown indefinitely in the
laboratory.
 Normally, plasma cells produce antibody, so a particular cell line
that is not capable of producing antibody is chosen for this process.
 This cell line has a deficiency of the enzyme hypoxanthine guanine
phosphoribosyl transferase (HGPRT), which renders it incapable of
synthesizing nucleotides from hypoxanthine and thymidine, which
are needed for DNA synthesis.

 Production of Monoclonal Antibodies
 A mouse is immunized with a certain antigen
 Mouse mounts polyclonal response
 After a time, spleen B cells are harvested.
 Spleen cells are combined with myeloma cells in the
presence of polyethylene glycol (PEG), a surfactant.
 The PEG brings about fusion of plasma cells with
myeloma cells, producing a spleen/myeloma hybridoma.
 Also myeloma/myeloma and spleen/spleen
hybridomas formed.
 Only a small percentage of cells actually fuse, and
some of these are like cells—that is, two myeloma
cells or two spleen cells.

 Production of Monoclonal Antibodies
 After fusion, cells are placed in culture using a selective
medium containing hypoxanthine, aminopterin, and
thymidine (HAT).
 PEG has been removed from system to stop hybridization
 Culture in the HAT medium is used to separate the
hybridoma cells by allowing them to grow selectively,
since only they can synthesize nucleotides in this
medium.
 One pathway, which builds DNA from degradation of old
nucleic acids, is blocked, because the myeloma cell line
employed is deficient in the required enzymes HGPRT
and thymidine kinase.

 This leaves only the fused hybridoma cells,
which have the ability (acquired from the
myeloma cell) to reproduce indefinitely in
culture and the ability (acquired from the
normal B cell) to synthesize nucleotides by
the HGPRT and thymidine kinase pathway.

 Monoclonal antibodies are produced by
a clone of cells called hybridoma cells
 Contains two cell types, a spleen cell and
a myeloma cell
 Desired spleen cell–myeloma cell hybrids
need to be selected from the myeloma cell–
myeloma cell hybrids and the myeloma cells
alone
 The chosen myeloma cells don’t make
immunoglobulin

Monoclonal antibodies
 Selection of cells making desired Ab
 Cells are grown in 96 well plates
 Diluted so wells contain a clone derived
from one cell
 Supernatants are tested for
 Reactivity with the antigen
 Undesired cross reactivity
 Cells with desired specificity are grown up,
subcloned and frozen for use for years


Antibody Purification
 To purify any protein
 Solubility characteristics
 Molecular weight
 Binding affinities
 Charge

Antibody Purification
 Methods of purifying antibody
include
 Ammonium sulfate precipitation
 Affinity purification of antibody
 Specific antigen column chromatography
 Fc binding column chromatography
 Protein A,G, L

 Monoclonal antibodies were initially used for in
vitro diagnostic testing, and this use continues.
 Recently, monoclonal antibodies have begun to be
employed in delivering therapeutic agents in a
variety of diseases.
 This area of research in pharmacology is rapidly
expanding and is likely to continue to grow in
the future.


Unit 2-Lecture 1-Antibodies

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Unit 1-Lecture 4

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

 The segment of H chain located between the CH1

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

 IgG – 2γ H-chains 2L-chains

Contemporary Clinical Immunology and Serology

 There are four major subclasses,

Subclass Placental Complement Opsonic Half-Life

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

 IgD – 2δ H-chains 2L –chains

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

 The Side-chain theory

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology

Contemporary Clinical Immunology and Serology