CHAPTER

6
AntibodiesS
(Immunoglobulins)
6.1. INTRODUCTION
Antibodies, or immunoglobulins (lg), the magic bullets of the immune system, are
glycopro
teins formed by plasma cells in response to antigenic stimulation and counteract with
anti
gens with great specificity. They are found in blood serum and other body fluids such as
gastric secretions and milk. Senum containing antigen-specific antibody is called antiserum.
The chemical composition and structure of antibodies was revealed
by G. M. Edelman and
ANTIGEN
HEAVYCHAIN
ANTIGEN-ANTIBODY
BINDING SITE ANTIGEN
T
LIGHT CHAIN
LIGHT CHAIN
LIGHT CHAIN
HEAVY CHAIN HEAVY CHAIN
A
FIG. 6.1. B
Antibody molecule (A) T-shape antibody before it binds to antigens
after it binds to
antigens. and (B) Y-shape ann bod
 VTIBODIES(MAAUNOGLOBULINS)
awarded the Nobel prize in 1970 in physiology and medicii for this
M. Porterwho were
contribution.
contrn tibody or immunoglobulin molecules have molecular weight ranging from 1.50,000 to
Electron microscopic viewing reveals that the antibody molecules resemble
9,00,000 daltons. after
theletterT
before they bind to antigens (Fig. 6.1 A), while they resemble the
letter
6.I B). It is considered that the antibody-antigen binding causes a
Y
ntigens (Fig.
ding to antigens
gement in the T-shape structrre of the antibody molecule resulting in Y-shape thus
to complement-binding site of heavy chain for further reactions.
rcar more exposure
most human
proves have more than one antigen-binding sites. For convenience, molecules can
A n t i b
dies binding sites or are bivalent. Some bivalent antibody
possess two
ntibodiespossess
antibo form multimeric antibodies that have upto 10 bindingsites.
combine to f
6.2. BASIC STRUCTURE
of four
hantibody
Each antibody
(immunoglobulin) molecule has a basic structure composed
connected to each other by disulfide bonds. The four polypeptide chains
chains
polypeptide chain
"T or 'Y'
the form of flexible the
letters; is maintained by a hinge
flexibility
arTanged in the.
arearrangedstalk of the Y temed the crystallizable fragment (Fc) and contains the site at
weion. The IS
molecule can bind to a cell. The top of the Y consists of two antigen-
which the antibody with compatible epitopes or antigenic determinant at
inding fragments (Fab) that bind
antigen-binding
sites (Fig. 6.2).
ANTIGEN-BINDING
F R A G M E N T( F a b )
ANTIGEN
ANTIGEN BINDING
SITE
HEAVY CHAIN HINGE
REGION
LIGHT CHAIN -s-s VARIABLE
REGION
S-S-
CRYSTALLIZABLE CONSTANT
FRAGMENT (F) REGION
FIG.6.2. An antibody molecule structure. Note four polypeptide chains (two heavy and two light) joined
by disulfide bonds, and their different components.
Two of the four polypeptide chains of antibody molecule are identical to each other and
remaining two are also identical each other and
ire called heavy (H) chains,
are called
whereas the to
light (L) chains.
 72 IMMUNOLOGYAND MEDICAL
6.2.1. Heavy and Light Chains
MICROBIO
Heavy chains possess greater number of amino acids (approximately 440 amino
chain) and thus higher molecular weight (approximately 50,000 to 70,000
00 daltois acids is each
structurally distinct for each immunoglobulin class or subclass. Light chains mand daltons)
number of amino acids (approximately 220 amino acids in each chain)
and less
molecular weight (approximately 25,000 daltons). Both heavy and light chains lo
contain two different regions, constant
region (C) and variable region (V). The 6,3
region of heavy and light chains have amino acid sequences that do not
between antibodies of the same class but, the variable vary sipnie.ang
region of both the chainstly
dilferent amino acid
sequences in different antibodies. The constant region of
and light chains contain both the
homologous units of 100 to 110 amino acids; each such unit cally
constant domain (CH and
C, respectively). Likewise, the variable region of
chains possess variable domain (Va
heavy and li
and VL respectively). Each light chain has a ght
variable domain (V) and a
single constant domain (C), whereas each heavy chain sinol
a single variable
domain (Vh) and three, sometimes four, constant possese
sses
and sometimes, Cy4). Within each of both domains (CI, C2, C.3
type of domains (constant and variable),
bonds forma loop of
approximately 60 amino acids. disulfide
6.2.2. The
Antigen-Binding Site
Immune system possesses the
capacity to recognize and bind countless antigens and each
antigen is bound by unique
a
antigen-binding
formed by cooperative interaction
site. The antigen-binding site of all antibodies is
between the variable domains of both
chains (Fig. 6.3). The variable domains of both chains interact to form a
heavy and light
binds strongly but molecular site that
noncovalently with the antigen. The strength of this
antigen-binding affinitry. An antibody is said to bind binding
with high affinity if the
is termed
strongly and is heldtightly by the antibody. antigen interacts
6.3. ANTIBODY FUNCTION
Antibody molecule shows a different role
binding fragments (Fab)
played by each of its two
regions, the
(Fab)
and the
crystallizable fragment (Fc). Its antigen
region functions to bind antigen, whereas the antigen-binding fragments
various cells ofcrystallizable
mediates binding to tissues of the fragment (Fc) region
cytic cells, or the first host, the immune
component of the system, certain phago-
antigen this normally does not
complement system. When antibody molecule binds
mark and identify the
cause destruction of the
antigen rather the antibody serves to
antigen for
destroy the antigen. However, immunologic attack and to activate immune responses that
the
action takes place in different binding of antibody to antigen, i.e.,
immunity inside the body of theways, and is the central dogma of antibody-mediated antigen-antibody inter
of
antigen-antibody interactions in
host. The
important functions attributed to antibodies(humoral)
the host body : by way
formation, (3) opsonization,
(4) complement fixation, neutralization,
are (1) (2) immune
mediated and (5) complex
cytotoxicity (ADCC). In addition, antibodies also contribute antibody-dependent cel1
hypersensitivity,
1on. All these autoimmunity, and immunodeficiencies by way of
in the
causation of
described in some detail inantigen-antibody
functions of antibodies are interac-
section 8.2.
 TIBODIES (IMMUN
UNOGLOBULINS) 73
ANTIB
HEAVY CHAIN
S-S- S
S-
LIGHT CHAIN s-s s-s
s-S 3 -
-
CH2
LOOP
GD
C3
and light chains of an antibody molecule showing constant and variable domains each
riC 6.3. Heavy
of which possess loops
OF ANTIBODIES (IMMUNOGLOBULINS)
6.4. CLASSES (TYPESs)
(antibodies) possess same basic structure as described earlier, their
All immunoglobulins in amino acid
variations in
phvsicochemical properties vary considerably because of sequence
chains. Therefore, on the basis of their physicochemical properties,
their heavy polypeptide
immunoglobulins (gs) are divided
into five different classes, namely, immunoglobulin G
the
M immunoglobulin D (lgD), and
(IgG), immunoglobulin A (lgA), immunoglobulin (lgM), the fact that immunoglobulins have
immunoglobulin E (lgE). This nomenclature is based on These
five different amino acid sequences in the constant domains
of the heavy chains (CH).
amino acid sequences are designated by lower case Greek letters gamma (Y). alpha («), mu
(4), delta (8), and epsilon (¬).
6.4.1. Immunoglobulin G (lgG)
immunoglobulin in human serum accounting for 80%
occurring
gG is the most abundantly
of the immunoglobulin pool. This antibody is termed "maternal antibody" because it is the
only class of antibodies that crosses the placenta and confers immunity upon
the foetus that
lasts for the first months after birth. IgG has a molecular weight of about 150,000 Da; the
Da. Each heavy
OCular weight of its heavy chain is 50,000 Da and of light chain is 25,000 A
chain consists of about 440 amino acids, while each light chain has
functional IgG antibody consists of two antigen-binding units, each unit consisting of one
about 220 amino acids.
he and one light chain. Therefore, IgG are bivalent and can bind two identical
epitopes.
 IMMUNOLO0GYAND MEDICAL
74
human, namely, IgG1, IgG2, IgG3
CROBIOLOG
and IgG4. he
and
Thee
There are four subclasses of IgG in
different chemical compos
subclasses mainly differ from each other in possessing sition in the
heavy chain and the number and arrangement
of interchain disulfide bonds (Fig. 66.4). 6nh
onds (Fie.
gG antibodies in serum are IgGI antibodies, whereas 23% are the IgG2 ones. nes. The 65 oo
These
antibodies perfom different biological functions. IgG3 ana
For convenience, IgGl and
are anti-Rh antibodies and, upon recognition of their specific antigens, bind to d
IgG3 antsubclas
ibodie
rece
expressed on monocytes and macrophages and
make them better phagocytes.
ytes. IgG2 anePlo
tibodies
are opsonic and develop in response to antitoxins. IgG4 antibodies, howe
skin-sensitizing immunoglobulins.
HINGE REGION DISULPHIDE BONDS
CARBOHYDRATE
SIDE CHAINS
IgG1 IgG2 igG3 lgG4
FIG. 6.4. Subclasses of immunoglobulin G (lgG) showing differences in arrangement and number of
disulphide bonds (-s-s-). The latter are shown by thin lines joining the two heavy chains of
the immunoglobulins.
6.4.2. Immunoglobulin M (lgM)
IgM is the largest antibody and the third most abundant (10% of total antibodies) in human
serum. It appears to have been the first
type to arise during evolution, being the most
abundant in primitive vertebrates. IgM is usually a polymer of five monomeric units
(pentamer), each possessing two heavy chains and two light chains Fig. 6.5. The monomers
are arranged in a
pinwheel array held
DISULFIDE together by disulphide bonds and a special
BOND
J-chain (joining chain). In addition to
A three constant domains
all heavy chains
(CHl, CH2, CH3),
possess a fourth constant
domain (CH4). IgM is the first immu-
noglobulin made during B-lymphocyte
maturation and is
J-CHAIN bound antibody on
expressed as membrane
secreted into serum B-Iymphocytes, IgM is
during
antibody response following primary
the introduc
tion of an antigen in the
body. Since this
antibody is so large, it does not leave the
blood-stream or cross the
FIG. 6.5. The pentameric
are generally of low placenta. IgMs
affinity but high
structure of immunoglobulin vlany
M (lgM). (Srengn of
Einding to antigen). Its
strength of
binding antigens
(avidity)
is
 IBODIES
(IMMUNOGLOBULINS 75
the
valente of the pentameric IgM molecule; 10
high valk en-binding sites are
enhanced by with antigen.
availat f o r interaction
sides their pentameric their pentameric torm, about 59% or less of IgMs exist in hexameric form. It is
terial cell wall antigens such as gram-negative lipopolysaccharides directly
bacterial
suggested1that
R-Iymphocytes to synthesize hexameric IgM, which lack a J-chain. This form of
imulate B - l y
complement up to twentytold more effectively than does the normal pentameri
vates
g h
form.
Immunoglobulin aglobulin M (TgM) molecules agglutinate gram-negative bacteria, activate
Iment by the classical pathway, and enhance the ingestion of pathogens by the process
complement b y t
o f
p h a g o c y t o s i s .
6.4.3.
Immunoglobulin A (IgA)
second m o s t
abundant (15% of total antibodies) in hum and occurs in body
is the from the
gfluids such ch as saliva, tears, breast milk colostrum, and mucosal secretions
a s t r o i n

respiratory, and genitourinary tracts. All of these mucosal surfaces are

t e s t i n a l ,
mucosal-assoCiated lymphoid tissue (MALT) that produces IgA. Initially
ciated with mu
of two heavy and two light chains but, when transported from the
are a monomer
IgAs tissue (MALT) to mucosal surfaces, acquire a protein called
osal-associated lymphoid
ucosal-associate
consists of
nponent' and get moditied. The modified lgA becomes a dimer, i.e.,
'secretory component
molecules covalently linked by a J-chain peptide and the protein 'secretory
IgA
and is now called secretory 1gA (slgA) (Fig. 6.6). The secretory component
two
component
across membranes. Since the mucosal surfaces total
about
ratein adds in transport of igA of their number far exceeds
00 M, large amounts (@ g/day) secretory IgAs produced;
10 are
of IgG in the serum that are produced
the number
individual. However, IgA is in an
normally@ 5g/day monomer.
serum as a
also present in
A (slgA) protect the
Secretory immunoglobulin
microbial pathogens by forming
surface tissues against
in
immune barrier. For convenience, slgAs present
/J-CHAIN
breast milk protect nursing new-borns; slgAs present
in intestine bind to protozoan parasites (e. g.,
SCRETORY
Entamoeba histolytica), bacteria, and viruses and thus COMPONENT
surfaces andd
prevent their adherence to mucosal
invasion of host tissues by them. This phenomenon is
referred to as immune exclusion. In addition, slgAs
bind to antigens forming antigen-slgA complexes
within the mucosal layer of small intestine. These
complexes are excreted through the adjacent
ptnelium into the gut lumen and, in this way, the FIG. 6.6. Secretory lgA (immunoglobuin
äccess of immune complexes to the circulatory system dimer) structure. Note the A
presence ot J-chain and
s decreased. slgAs also play a considerable role in the secretory component in it
alternative complement pathway.
76
IMMUNOLOGYAND MEDIC MICROB
AICROBIOLOG
6.4.4. Immunoglobulin D (lgD)
in low concentrations
(only 0.29% of total antibodiea
Inmunoglobulin D (lgD) occurs structure is similarh
m o n o m e r s and
their monomeric
These antibodies are
blood serum.
susceptible to proleoiytic enzymes a
molecules are short-lived, being particularly ahn
gD
not fix complement
and fail to cross placenta. They
heat. These antibodies do bind antigen, and sio
with IgM on the surface
of B-lymphocytes,
Occur in combination found that 1gD is espea
been
formation. It has
to initiate antibody
B-lymphocytes and, most probablv
from B-lymphocytes
abundant on memory cells differentiated
play
important role in secondary antibody
response.
6.4.5. Immunoglobulin E (lgE)
in extremely small
amounts (only oftotal
0.002% antibodiec.
and
TgE occurs in blood serum concentration, are
classic skin-sensitizing
antibodies, despite low and
are monomeric. These (allergies) are mediated
anaphylactic antibodies vecause
immediate-type 'iypersensitivities
antibodies (reagins). The molecu.
dby
called allergic
them. They are therefore popularly antibodies because, like IeM
other
weight of an IgE is significantly
higher than most bind lgE to special
additional constant
domain helps
constant domain. This
possesses a fourth
can also be activated).
When two lap
cells (basophils and eosinophils
receptors on mast
these cells are cross-linked by
binding to the same antigen. th
molecules on the surface of and otner pharmacological
releases histamine, heparin,
cells degranulate. This degranulation contraction of smooth muscla
and
mediators that cause dilation
of local blood vessels
reactions such as broncheal asthama,
allergic rhinitis, etopic eczema, cte
resulting in allergic
and gut hypermotility.
It also stimulates eosinophilia
chemical, and immunological properties of
Table 6.1 summarizes important physical,
classes of immunoglobulins.
IgG, IgM, IgA, IgD, and IgE
VARIANTS
6.5. IMMUNOGLOBULIN (ANTIBODY)
variants, which can be classified as:
Classes (types) of immunoglobulins (antibodies) possess
These variants occur due to variations in
() isotypes, (2) allotypes, and (3) idiotypes. the antibody
located in characteristic portions of
antigenic determinants or epitopes
molecules.
6.5.1. Isotype
Isotype variants arise due to isolypic determinants in the constant region that collectively
a
define each heavy chain class and subclass and each light chain type and subtype within
species (Fig. 6.7). Each isotype determinant is encoded by a specific constant-region genes
and all members of a species possess the same set of constant-region genes. Each norma
individual within a species expresses therefore all isotypes of an antibody in the seru
Diferent species have different constant-region genes and express different isotypes or
 TABLE 6.1
Important properties ofdifferent classes of immurnoglobulins (lgs)
Property ImmunoglobulinClasses
igG IgM l9A igD lgE
I. Distribution Extracellular fluid; blood Blood and lymph; Secretions (saliva, Blood and lymph; Blood and
and lymph; crosses monomer is B colostrum, cellular B-lymphocyte lymph; binds to
placenta lymphocyte- and blood fluids); surfaces mast cell surfaces
surface receptor monomer in blood
and dimer in
secretions
2. Heavy chain Gamma (Y) Mu () Alpha (o) Delta (8) Epsilon (8)
3. Total percentage 80 10 15 0.2 0.002
4. Mean serum concentration 13.5 1.5 3 0.03 0.00005

(mg/m)
5. Molecular weight (mass) 150,000 970,000 160,000 185,000 188,000
of entire molecule (Da)
6. Molecular weight (mass) 51,000 65,000 56,000 70,000 72.000
of heavy chain (Da)
2 10 2 2 2
7. Antigen-binding sites
(valency)
8. Half life (time required for 23 6 3 2
half of the antibodies to
disappear) in serum (days)
9. Complement activation
+++
:Classical pathway
Alternative pathway 7-10 12
10. Percentage of
carbohydrate
11. Placental transfer Involved in
First antibody to Secretary Minor circulating
12. Other main features Most abundant and major allergic reactions;
circulating antibody; four appear after antibody; protects antibody;B
resistant to
subclasses (1gG1, IgG2, immunization; cxternal surfaces lymphocyte helminths
recognition of
very effective
IgG3 and IgG4);
agglutinator antigen
neutralizes toxins;
opsonizes bacteria
maternal antibody
78 IMMUNOLOGYAND MEDICAL MICRORIA
oLOG
ISOTYPIc
DETERMINANTS-
B
A
FIG. 6.7. Isotypes. (A) Isotype of immunoglobulin G1 (lgG1) subclass and (B)
immunoglobulin M (lgM) class. Note that isotype deteminants of these immunoglohul isoty
ns ae
encoded by heavy chain constant region genes.
antibody. This is the reason why an antibody from one species injected into another sDee.
ecies i
immune response.
recognized as foreign and subjected to
6.5.2. Allotype
variants of an antibody are determined by the sum of the individual allot.
Allotype
determinants (amino acid differences) of the antibody (Fig. 6.8). Although all individual otypi
alleles exit for some of these pena
carry the same set of isotype genes, multiple
speciesalleles
These encode subtle amino acid differences occurring in some, but not all, individu-
of a species. These amino acid differences are called allotypic determinants. Allotypes ha
beea characterized for all four IgG subelasses (lgG1, IgG2, 1gG3 and IgG4) and for one Ie
bclass in humans. Antibody to allotypic determinants can arise when antibodies from o-
ndividual of a species are injected into another individual of the same species who cari
from blood transfusion.
allotypic determinants. They can also be produced
a
different
TV
ALLOTYPIC
DETERMINANTS
B
strain A and (B) of strain B. Note that
FIG. 6.8. Allotypes. (A) Allotype of immunoglobulin G1 (igG1) different alleles=
allotypic determinants are subtle amino acid differences encoded by
isotype genes.
6.5.3. Idiotype
Tdiotype variants refer to individual specific antibody molecules that differ in
hypervariable region of antigen-binding fragments (Fab) of both the heavy and light c
variable domain (VH) and
(Fig. 6.9). The unique amino acid sequence of heavy chain
 ANTIB,
oDIES MMUNOGLOBULINS)
79
edomain (V)
able doma of a
given antibody can function not only
c h a i n v a r
also
as a set of
set
as an
antigen-binding
of antigenic delerminants, called idiotypic determinants. Each individual
ite
but erminant of the variable domain is called as an idiotope. Each antibody wii.
antigenic einle idiotopes, and the sum of the individual idiotopes is called the idiotype of the
oresent multiple idiot
Convenience,
For convenience, all the antibody molecules produced by individual B-lymphocytes
antibody.
the
derivedfrom the same clone possess identical amino acid sequences of variable domain, they
erefore
havethe.same idiotype.
all
IDIOTYPIC DETERMINANTS
OR IDIOTOPES
'.:
9 , Idiotypes. (A) ldiotype of lgG1 antibody molecule produced against antigena and (B) idiotype
of lgG1 antibody molecule produced against antigen b. Note that the idiotypic determinants
(or idiotopes) are generated by the unique amino acid sequence of heavy chain variable
domain (VH) and light chain variable domain (V).
6.6. MECHANISMA OF ANTIBODY FORMATION : CLONAL
SELECTICON THEORY
As discussed earlier in Section 4.2.1, these are the B-lymphocytes that produce antibodies in
the body. Various theories have been proposed regarding the formation of antibodies, it is the
clonal selection theory which has gained wide support. This theory states that there are a
variety of B-Iymphocytes present in the immune system. These lymphocytes produce a small
number of antibody molecules without any antigenic stimulation, and these antibody
molecules integrate into the cytoplasmic membrane of their producer lymphocyte to serve as
receptor site for specific antigen. When specific antigens enter the immune system, they
interact only with complementary antibody-receptor site of B-lymphocyte. In this way, such
B-lymphocyte is "selected out" or "differentiated" by the union of specific antigen and its
the complementary antibody. This "selected out" or "differentiated" B-lymphocyte is stimulated
o undergo multiplication leading to clones of plasma cells which synthesize and secrete a
of antubodies complementary to the specific antigens that have entered the immune
system. In fact, the "selected out" or "differentiated" B-lymphocytes initiate multiplication
i n g two different cell populations: the primary B-lymphocytes and the secondary B-
the cytes. The primary, in response to antigenic stimulation, divide and transform into
ins 4cells which enter into the process of antibody formation, but the secondary B-
ght
g pytes do not. The latter circulate actively from blood to lymph and liver, and
 80
IMMUNOLOGYAND MEDICALLMICR0
MICROBIOLO
constitute memory cells. These memory
cells, however, transform into plasma cell
years later, and ento
they are to
exposed antigenic stimulation, perhaps
subsequent nter into
process ofantibody formation (Fig. 6.10A).
into antibody-synthesizing mature plae.
The B-lymphocytes get transformed revealed that a transformatinma Cel
6.10B). It has been
through a prolonged process (Fig. successive cell generations is requiredod
about five days involving atleast eight cells. With each cell DeO h
the B-lymphocyte
formation of mature plasma cells from io
ribosomes and endoplasmic
reticulum. By the
there is a progressive development of
much increased and its
entire protein svnt d
the RNA content of the plasma cell is very
reticulum cisternae are filled with i
machinery is so activated that the endoplasmic
It is estimated that about 90-959
them.
molecules, and the plasma cells rapidly secrete the
SPECIFIC ANTIGENS
PLASMA CELL
-CYTOPLASM
OoOoOOO000
SECONDARY PRIMARY B-LYMPHOCYTE
B-LYMPHOCYTE DAY
1st GENERATION
PLASMA CELL
OODQ 2nd GENERATION RIBOSOMES
MAMORY CELLS
O O O Q 3rd GENERATION
DAY
PLASMA CELL- OOOO4h GENERATION
ENDOPLASMIC
sth GENERATIONOOOO RETICULUM
DAY
3
6thGENERATION OOOC ANTIBODIES SYNTHESIZED
WITHIN CISTERNAE OF ER
DAY
7hGENERATION OOQO 4
MATURE PLASMA CELL
8th GENERATION OO00 DAY BSECRETED ANTIBODIES
CLONE OF PLASMA CELLS
THAT PRODUCES ANTIBODIES
COMPLEMENTARY TO THE
SPECIFIC ANTIGEN
A B
revealing
FIG. 6.10. Clonal selection theory. (A) Diagrammatic representation of clonal selection theory
the "differentiation" of B-lymphocyte, its stimulation to divide and produce clone of plasma
cells and (B) transformation of B-lymphocyte (newly differentiated plasma cell) into mature
plasma cell (antibody-synthesizing cell) that secretes antibody molecules.
ANTIBOD
I E S(IMMUNOGLOBULINS)
B M U
duced in plasma 81
sma cells
gives rise
o t a l
p r o t e
eted per plasma cell per second. to antibodies, and about
out 10,000 antibody
olecules.
ut the circulatory system are in However,
operation for the obviously thousands
I sthroughoutthe
of plasma
cells
g i v e nt i m e

of productionat antibodies any

Questions
antibodies ? Why a T-shaped
Describe the basicsstructure ofantibody
What are
molecule becomes
1 antigens
?
an
antibody molecule.Y-shaped ater binding to
a any classes of antibodies are
dies of antibodies belonging to fwo recognized,
2. How m a n y
and why ?
most
Describe the structure and
be key differences and similarities betweenabundantly occurring classes in human serum.
p r o p e r t i e s
Describ
IgG, IgA, and IgM
3.
mmunoglobulin is called maternal antibody, immunoglobulins.
4 different variants of immunoglobulins and why ? Give a concise account or
Giv a
sumimariz rized account of different properties of the classes of
5.
tabularform immunoglobulins in a
tis clonal selection theory ? Desçribe the mechanism
theory.
of antibody formation based on this
Writ notes () heavy and light chains, (i) antibody function, () IgE, (iv) J-chain,
7.
idiotypes, (V7) Isolype, and (Vi) plasma cells and memory cels.