ANTIBODY Flashcards
humoral immunity is based on the secretion of production of what component?
anti bodies
The fully differentiated type of lymphocyte that is The main objective of the ____is to
release or secrete antibodies
plasma cells
t cell or b cell?
humoral immunity
b cell
Cluster differentiation or surface marker
that remain on the cell surface throughout
the subsequent developmental stages of the B CELL:
CD19, CD24, and CD45R
____ is the surface protein that is found on
both activated cells and B cells and act as a
receptor for IL-2
CD25
antibodies are also known as the
Immunoglobulins
what cytokine is responsible and acting as a receptor for the surface protein that is found on both activated cells and b cells
interleukin 2
Glycoprotein found in the serum portion of the
blood.
immunoglobulins
where can we found the antibodies?
serum portion of the blood
what is the composition of the immunoglobulins.
give the percentage each composition
82-96%→polypeptides (protein)
2-14%→carbohydrates
HWO CAN WE BE ABLE TO DISTINGUISH THE BEHAVIOR OF THE IMMUNOGLOBULINS?
THROUGH ELECTROPHORESIS
materials of substances we can use for electrophoresis that is based on pH
cellulose acetate and citrate agar
what is the pH level of cellulose acetate we used for electrophoresis
alkaline - 8.6
what should be the pH level if we will use the citrate agar for electrophoresis
6 - 6.3 - acidic
In what region we can found the immunoglobulins?
gamma region (y)
since we can found the immunoglobulins in gamma region, we can call it as well as
gamma globulins
technically, what is the pH level we need for electrophoresis?
8.6
(transes based - we use agarose gel if 8.6 pH is needed)
immunoglobulins plays an essential role
what are the functions:
antigen recognition
immune response
capable during opsonization
complement activation
what are the classification of the immunoglobulins
GAMDE
IgG
IgA
IgM
IgD
IgE
___is the most abundant protein when it comes
to the serum electrophoresis
Albumin
Immunoglubulin is designated as ___
Ig
what is the arrangement of the protein or region in the serum electrophoresis
start from albumin to gamma region
albumin
alpha 1 globulins
alpha 2 globulins
beta globulins
gamma region
the arrangement of the regions/proteins in the serum electrophoresis is based on ___
net charge
what are the proteins under alpha 1 globulins
Alpha-1 Antitrypsin (AAT)
Alpha Fetoprotein (AFP)
what are the proteins under alpha 2 globulins
ceruloplasmin
haptoglobin,
alpha-2 macroglobulin
what are the proteins under beta globulins
transferrin
hemopexin,
complement system
fibrinogen
lipoprotein (LDL, HDL, VLDL)
There is a possibility of an abnormal pattern in serum
electrophoretic activity called the ___, which is in line with the beta
region
Beta–gamma bridging (curved)
it can be used as a screening test for certain clinical disease
electrophoresis
what disease is associated with an abnormal pattern in line with the Beta region
liver cirrhosis
The spike pattern within the gamma region is associated with ___
multiple myeloma (elevated plasma
protein)
which immunoglobulin is elevated for patients with multiple myeloma
IgG immunoglobulin gamma
Common/significat protein found in URINE with MULTIPLE MYELOMA is called
Bence-Jones proteins
Bence-Jones proteins are mainly associated with which chain of the antibodies
Light chain
The Bence-Jones proteins are distinguished by
precipitating for about____ and will dissolve at
___.
60 Celsius; 80 Celsius
what will happen to a bence-jones protein in 60 degree celsius?
it will precipitate
what will happen to a bence-jones protein in 80 degree celsius?
it will be dissolve
All immunoglobulin molecules are made up how many basic chain of polypeptide nit?
4 basic chain
4 basic chain of polypeptide unit for immunoglobulin is made up of how many heavy and light chain?
2 large heavy chain
2 small light chain
The chains of immunoglobulin are held together by noncovalent forces
called the ____
disulfide linkage/bond
The four chain polypeptides can be connected
through ___
disulfide linkage/bond
Structure of Immunoglobulins was first describe by two scientists.
who are they?
Gerald Edelman and Rodney Porter
disulfide linkage/bond is also called as
disulfide interchain bridges
which immunoglobulin do Gerald Edelman and Rodney Porter studied?
Ig G - immunoglobulin gamma
after ultra centrifugation of Ig G- they were able to find the ___
sedimentation coefficient value
what is the sedimentation coefficient value of IgG
7s (Svedberg unit)
___ indicates the sedimentation rate in an analytical
ultracentrifuge
Svedberg unit
before they used the analytical ultracentrifugation, they need to ___ the Ig G
purify
On obtaining a purified preparation of
IgG. Edelman used ___to unfold the molecule.
7M (7 Molar Urea)
reagent used in order to unfold the Ig G molecule
7M (Molar Urea)
Once the Ig G molecule is unfolded, the exposed sulfhydryl bonds could be cleaved by a reducing agent such as ____
2-Mercapthoethanol
2-Mercapthoethanol will reduce the exposed bonds which is the
bonds
after the second ultracentrifugation, we will be able to come up to a sediment coefficient of ___
3.5 S and 2.2 S
3.5 S fraction has a molecular weight of approximately ___ Da.
50,000
2.2 S fraction has a molecular weight of
approximately ____Da
22,000
3.5 S fraction is designated to which chain?
heavy chain.
2.2 S fraction is designated to which chain?
Light chain
Gerald Edelman and Rodney Porter won the novel
prize in ___in ____
They were the first ones to describe the structures
of immunoglobulins.
1972 ; Physiology and Medicine Practice.
This is used to determine the structure of the immunoglobulin
ANALYTIC ULTRACENTRIFUGE
What are the regions of immunoglobulins
Fab and Fc region
FAB region - FAB means
Fragment antigen binding
FC region - FC means
Fragment crystallizable
who introduced papain digestion?
Rodney Porter
Papain digestion is Cleaves antibody into three fragments, what are those?
2 Fab
1 Fc
a type of fragment that has
no antigen binding ability. It is now known to
represent the carboxy terminal halves of Two heavy chains that are held together by SS bonding
Fragment crystallizable (Fc region)
a fragment that is mainly associated with the
antigen binding
Fab region - fragment antigen binding region
what are the fragments found in pepsin digestion
1fab and 1 fc
immunoglobulins that has
2 domain in light chain
4 domain in heavy chain
GAD -
IgG
IgA
IgD
immunoglobulins that has
2 domain in light chain
5 domain in heavy chain
EM -
IgE
IgM
Each Fab Fragment of Papain has how many chains
1 L chain and ½ of H
chain
Each FC Fragment of Papain has how many chains
two halves of H chain
Each FAB Fragment of pepsin has how many chains
2 L chain and two halves of H
chain
Each FC Fragment of pepsin has how many chains
two halves of H chain
The structure of light chains is not fully discovered
until the discovery of an abnormal protein produces
by patients with ____.
multiple myeloma
Analysis of several Bence-Jones proteins revealed
that there were two main types of L chains.
what are those?
kappa and lambda
type of light chain
Kappa is designated in what chromosome?
chromosome 2
type of light chain
lambda is designated in what chromosome?
chromosome 22
amino acid of kappa
200
amino acids of lambda
220
The FC regions of pepsin is ___
disintegrated into smaller pieces
the fragment associated with the variable region
FAB
the fragment associated with constant region
FC
variable regions associated with the FAB is located in the
amino terminal end
constant regions associated with the FC is located in the
carboxyl terminal end
a chain that detects the immunoglobulin class
heavy chain
Constant regions of the H chain are unique to each
class and give each immunoglobulin type its name.
IgG has a/an -__
IgM has a/an __
IgE has a/an - __
IgD has a/an - ___
IgA has a/an - __
IgG has a/an - Gamma chain “ɣ”
IgM has a/an - Mu chain “μ”
IgE has a/an - Epsilon chain “ɛ”
IgD has a/an - Delta chain “ẟ”
IgA has a/an - Alpha chain “α”
what are the ANTIBODY VARIATION
isotype
allotype
idiotype
the identity of immunoglobins are the same but they have unique characteristics given by what region
variable region - as they have the capacity during the antigen binding
a region associated on how they attached to a particular antigen - will provide unique characteristics as well to the antibody
variable region
antibody variation that has
unique amino acid sequence that is
COMMON to ALL immunoglobulin molecules of a given
class in a given species
Isotype
antibody variation that has
MINOR VARIATION of these sequences, some immunoglobulins are present but not with the others
Allotype
In allotype, it is based on what region of an immunoglobulin
constant region
antibody variation that has subclasses
Allotype
immunoglobulins that belongs in allotype variation
IgG and IgA
IgG has four subclasses and IgA
has two subclasses
a type of light chain that is an example of allotype
kappa chain
antibody variation that has
– variations in the variable region
Idiotype
Constant region is designated as ___ in Heavy chain
CH1, CH2, CH3
The segment of Heavy chain located between the CH1
and CH2 regions is known as the ___
hinge region
In heavy chain, the hinge region is can be found between what regions?
ch1 and ch2
amino acids for hinge region is the
proline
the amino acids, proline, for heavy chains allows___
it allows for FLEXIBILITY that makes the
ANTIGEN BINDING SITES WORK INDEPENDENTLY
immunoglobulins that has hinge region
IgG, IgD, IgA
immunoglobulins that has NO hinge region
IgE, IgM
a particular factor which we can determine the antigen binding site if an immunoglobulin
valence
what are the basic immunoglobulin structures?
monomer
dimer
polymer
how many binding sites do monomer has?
2 binding sites
how many binding sites do dimer has
4 binding sites
how many binding sites do polymer has
more than 4
an example of monomer
IgM (surface area of B cells),
IgE
IgG
serum IgA
IgD
an example of dimer
Secretory IgA
an example of polymer
IgM – has 10 valence
how many valence do IgM has?
10 valence - 10 binding sites - 5 sungay
an immunoglobulin that has 23 days half life
IgG
___is the most predominant immunoglobulin in
humans
IgG
IgG constitutes how many percent of the total serum immunoglobulins
70% to 80%
the mnemonic ____
(from most
predominant
to LEAST)
GAMDE
IgG is best at what reaction due to it’s relatively small size, this reaction is better than agglutination
precipitation reaction
There are four major subclasses of IgG
IgG1, 67%;
IgG2, 22%;
IgG3, 7%;
IgG4, 4 %
The subclasses of IgG differ mainly in the number and position of the disulfide bridges between the γ
chains. (in conjunction with heavy-to-heavy chains)
give the corresponding disulfide bonds of each subclasses
IgG1 – two disulfide bonds
IgG2 – four disulfide bonds
IgG3 – five disulfide bonds; has the largest hinge region
IgG4 – two disulfide bonds
which IgG subclass has the largest and the most number of disulfide bonding and hinge region?
IgG3
Which immunoglobulin can cross placenta?
IgG
which subclasses of IgG can cross planceta?
all IgG can cross except for IgG2
which subclasses of IgG is the most efficient one for crossing placenta?
IgG1
can IgG helps in complement fixation?
yes, but the IgM is the special one for that
which subclass of IgG can’t help with complement fixation?
IgG4
can IgG react with agglutination reaction?
Yes, but not efficiently as they are small
what are the characteristic of IgG
precipitation reaction
little complement fixation
Opsonization
Neutralization of toxins and viruses
Participation during agglutination (with enhancement medium)
which serologic reaction do IgG is the best?
precipitation reaction
a reaction in which the soluble antigen reacts to the small antibody
precipitation reaction
an immunoglobulin that needs an enhancement region to perform with agglutination reaction
IgG
