2020 Biochem Activity 13

NAME: HERNAEZ, GABRIELLE JOHN R.
RATING: __________________
GROUP NO. 2- NOLA PENDER DATE: 12/12/20
ACTIVITY 11
IMMUNOGLOBULINS
Immunoglobulins, also known as antibodies, are glycoprotein molecules produced by plasma
cells (white blood cells). They act as a critical part of the immune response by specifically
recognizing and binding to particular antigens, such as bacteria or viruses, and aiding in their
destruction. The antibody immune response is highly complex and exceedingly specific. The
various immunoglobulin classes and subclasses (isotypes) differ in their biological features,
structure, target specificity and distribution. Hence, the assessment of the immunoglobulin
isotype can provide useful insight into complex humoral immune response. Assessment and
knowledge of immunoglobulin structure and classes is also important for selection and
preparation of antibodies as tools for immunoassays and other detection applications.
The various antibodies produced by plasma cells are classified by isotype, each of which differs
in function and antigen responses primarily due to structure variability. Five major antibody
classes have been identified in placental mammals: IgA, IgD, IgE, IgG and IgM. This
classification is based on differences in amino acid sequence in the constant region (Fc) of the
antibody heavy chains. IgG and IgA are further grouped into subclasses (e.g., in human IgG1,
IgG2, IgG3, IgG4, IgA1 and IgA2) based on additional small differences in the amino acid heavy
chain sequences.
Based on differences in the amino acid sequence in the constant region of the light chain,
immunoglobulins can be further sub-classified by determination of the type of light chain (kappa
light chain or lambda light chain). A light chain has two successive domains: one constant
domain and one variable domain. The ratio of these two light chains differs greatly among
species, but the light chains are always either both kappa or both lambda, never one of each.
Determination of individual subclasses is relevant in assessing primary immunodeficiencies or

immune responses, especially if the total IgG or IgA concentration is not altered or elevated.
I. LEARNING OBJECTIVES:
At the end of the exercise, the students should be able to
1. Draw a schematic diagram of immunoglobulin.
2. Know the different classes of immunoglobulins, and their characteristics and functions.
II. MATERIALS
Work sheet Biochemistry book E-article/E-book on Biochemistry
III. PROCEDURES
1. Draw a schematic diagram of immunoglobulin with label of its parts. Give the function or
role of each part.
2. Fill up the table with the classes of Immunoglobulin with their characteristics and
functions.
IV. RESEARCH QUESTIONS

1. Schematic diagram of immunoglobulin
2. Parts of the immunoglobulin and their function/s.
 Immunoglobulin are heterodimeric proteins comprise of 2 heavy (H) and two medium
(L) chains are immunoglobulins. They can functionally be classified into vector (V)
domains that bind antigens and constant (C) domains that determine effector roles,
such as complement activation or Fc receptor binding. By means of a complex
sequence of gene rearrangement events, the vector domains are formed and can
then be subjected to somatic hyper mutation after antigen exposure to allow
maturation of affinity. Each V domain can be divided into three regions of sequence
variability, called regions deciding complementarity, or CDRs, and four regions called
structure regions, or FRs, of relatively constant sequence. The H chain's three CDRs
are combined to form the antigen binding site, as classically defined, with the three
CDRs of the L chain. Five major groups of heavy chain C domains exist. The
isotypes of IgM, IgG, IgA, IgD, and IgE are defined by each class. It is possible to
divide IgG into four subclasses, IgG1, IgG2, IgG3, and IgG4, each with its own
biological properties, and to divide IgA into IgA1 and IgA2 in a similar manner. To
activate altered effector activity while preserving antigen specificity, the constant
domains of the H chain can be switched to allow altered effector function while
maintaining antigen specificity.
3. Complete the table.
IMMUNOGLOBULIN CHARACTERISTICS FUNCTIONS OTHER INFORMATION
Immunoglobulin G IgG antibodies are  to help prevent  This is the most

(IgG) large globular proteins infections. common antibody.
with a molecular  It's also ready to  It's in blood and other
weight of about 150 multiply and attack body fluids and
kDa made of four when foreign protects against
peptide chains. It substances get into bacterial and viral
contains two identical γ the body. When you infections.
(gamma) heavy chains don't have enough,  IgG can take time to
of about 50 kDa and you are more likely form after an
two identical light to get infections. infection
chains of about 25 kDa, or immunization.
thus a tetrameric
quaternary structure. Normal Ranges
Adult: IgG 6.0 - 16.0g/L
Immunoglobulin M Structure is often  protects against  Found mainly in
(IgM) referred to as the IgM bacterial and viral blood and lymph
“monomer”, as it is infections. fluid.
analogous in some  its main function  The first antibody the
ways to the structure apparently is the body makes when it
of immunoglobulin G control of B- fights a new infection.
(IgG). cell activation. B-
Normal Ranges Adult: IgM
cells create IgM
0.4 - 2.5g/L.
antibodies as a first
line of defense.
Immunoglobulin A Expressed in mucosal  Bathes and protects  It’s found in the
(IgA) tissues. Forms dimers mucosal surfaces linings of
after secretion. from attachment of the respiratory
pathogens. tract and digestive
system, as well as in
saliva (spit), tears,
and breast milk.
Normal Ranges Adult: IgA
0.8 – 3.0g/L
Immunoglobulin E IgE is similar to IgG  Binds to mast cells  Found in small
(IgE) in structure, but IgE has and basophils and amounts in the blood.
two unique features: (1) triggers release of There may be higher
The epsilon (ε) heavy histamine and other amounts when the
chain has a high chemical mediator of body overreacts to
(12%) carbohydrate inflammation and allergens or is
content and has an some allergic fighting an infection
additional constant responses. from a parasite.
region (CH4).
Normal Ranges Adult: 150 to
1,000 UI/ml; but the usually
accepted upper limit is
between 150 and 300 UI/ml.
Immunoglobulin D IgD represents about  Believed to the cell  The least understood
(IgD) 0.25% of the total surface receptor of antibody, with only
serum immunoglobulins immunocompetent B small amounts in the
and has an Mr of cell; important in blood.
185,000 and a half-life activation of B cell.
of 2.8 days (131), Normal Ranges Adult: 14 to
similar to that of IgE 85 mg/liter (144), 10 to 112
(162). Its synthesis rate mg/liter (21), and 5 to 240
is at least 10 times mg/liter (97).
lower than that of IgA,
IgM, and IgG.
V. REFERENCE/
 Retrieved from https://kidshealth.org/en/parents/test-immunoglobulins.html

 Retrieved from https://www.ouh.nhs.uk/immunology/diagnostic-tests/tests-
catalogue/immunoglobulins.aspx#:~:text=Normal%20Ranges%20Adult%3A,IgM
%200.4%20%2D%202.5g%2FL
 Retrieved from https://pubmed.ncbi.nlm.nih.gov/4062142/#:~:text=Variations%20in
%20the%20upper%20limit,150%20and%20300%20UI%2Fml.
 Retrieved from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC95839/#:~:text=Many
%20reference%20intervals%20(%E2%80%9Cnormal%20ranges,mg%2Fliter%20(97).
 Retrieved from https://www.hopkinsmedicine.org/health/conditions-and-diseases/igg-
deficiencies#:~:text=Immunoglobulin%20G%20(IgG)%20is%20the,more%20likely%20to
%20get%20infections.
 Retrieved from https://www.antibodies-online.com/resources/16/679/anti-
immunoglobulin-m-igm-secondary-antibodies/
 Retrieved from
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670108/#:~:text=Immunoglobulins
%20are%20heterodimeric%20proteins%20composed,or%20binding%20to%20Fc
%20receptors.
 Retrieved from https://www.sciencedirect.com/topics/agricultural-and-biological-
sciences/immunoglobulin-e#:~:text=Immunoglobulin%20E%20(IgE)%20is%20the,region
%20(CH4).
 Retrieved from https://cvi.asm.org/content/7/2/131#:~:text=IgD%20represents%20about
%200.25%25%20of,IgA%2C%20IgM%2C%20and%20IgG.

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NAME: HERNAEZ, GABRIELLE JOHN R.

Determination of individual subclasses is relevant in assessing primary immunodeficiencies or

At the end of the exercise, the students should be able to

1. Draw a schematic diagram of immunoglobulin.

IV. RESEARCH QUESTIONS

2. Parts of the immunoglobulin and their function/s.

3. Complete the table.

IMMUNOGLOBULIN CHARACTERISTICS FUNCTIONS OTHER INFORMATION

Immunoglobulin G IgG antibodies are  to help prevent  This is the most

 Retrieved from https://kidshealth.org/en/parents/test-immunoglobulins.html

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