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produced in response to an antigen
what is an antibody
soluble b cell proteins
plasma cells
where do antibodies come from
specific binding
elimination
how antibodies work
body fluids and serum
where do antibodies located
detectable reaction
b cell receptors
detection and receptors
glycoproteins
antibodies are __
antibody
specific binding defines an __
immunoglobulin
__ refers to the activity
structural
immunoglobulin is a __
biological
antibody is a __
IgG
IgM
IgA
IgD
5 groups of immunoglobulins
heterogenous group
immunoglobulins are __ (20% of plasma proteins)
Electrophoretic Mobility
molecular weight
antigenic structure
immunoglobulin may be classified on the basis of
albumin
alpha
beta
gamma
in 1938, Tiselius and Kabat used electrophoresis to separate serum proteins into four distinct groups
molecular weight
using an ultracentrifuge, scientists measure how fast molecules sink (sedimentation)
Svedberg Units (S)
molecular weight is measured in __
Gamma
Meio
Alfa
Delta
Epsilon
antigenic structure
heterogenous glycoproteins
chain composition
the “y” shape
molecular architecture
heterogenous glycoproteins
large group of closely related glycoproteins with molecular weight of approx. 160 KDa
chain composition
4 chains
2 larger heavy chain (50-60 KDa)
2 smaller light chains (25KDa)
disulfide bonds
chains are joined by __ (-S-S-), creating the characteristic of “y” shaped apprearance
B-Cell Membrane
the carboxy (C) terminus of heavy chains is often inserted in the __
450 amino acids
alpha and gamma consist of __
550 amino acids
meio and epsilon consist of
3 constant domains + hinge reaction
gamma, alpha, delta contain __
4 constant domains and lack of hinge reaction
meio and epsilon classes contain __
110 amino acids
approx. ___ long per domain
kappa and lambda
two types of light chain characteristic
one variable and one constant
each light chain of two domains __
cattle or horse
95% lambda in __
rats/mice
95% kappa in __
humans
60% kappa in __
25 KDa
approx. __ per light chain
hotspot
complementarity determining regions (cdrs) is also known as __
complementarity determining regions
the variable region contains areas of extreme variability known as __
24-34
50-56
89-97
specific positions of cdrs
CDRs loops
stable peptide sequences located between the __
n-terminus
binding site formed by the groove created between light chains and heavy chains a their __
CH1 and CH2
hinge region located between __ domains; unique for each class and subclass
Fab regions
allows __ to swing freely around the central molecule
proline
region is hydrophilic and extremely rich in __
cysteine residues
hinge of IgD lacks __
papain
cleaves at hinge by hydrolysis of peptide bonds (proteolytic)
pepsin
cleaves towards the carboxy terminal side of disulfide bond
flexible hinges
an IgG molecule is characterized by three distinct globular regions linked by __
two fab regions
the “fragment antigen binding” arms
one fc region
the “fragment crystallizable” stalk that mediates biological effector functions
maintain stability
these regions allow the molecule to __ while performing complex recognition tasks
mechanical flexibility
The Hinge Region in the middle of heavy chains provides critical mobility. This flexibilty allows
the two fab arms to move independently to reach distant epitopes on an antigen surface
proteolytic vulnerability
The exposed peptide chains in the hinge are highly susceptible to breakage by proteases.
This structural feature is often exploited in laboratory settings to cleave IgG into Fab and
Fc fragments.
fab domains
fc domains
domain pairing
paired domain organization
fab domains
Each Fab consists of two pairs of domains: VH-VL (Variable) and CH1-CL (Constant). These chains are closely intertwined.
fc domains
Contains paired constant domains: CH-2-CH2 and CH3-CH3. IgE or IgM classses feature an additional CH4-CH4 pair.
domain pairing
The specificity of the antibody is determined by how these variable domains fold together to form a unique surface.
cdr specificity
A specialized groove is formed between the two variable domains, VH and Vl. This groove forms the actual antigen-binding site of the antibody.
two identical antigen-binding sites
Because immunoglobulins are bilaterally identical, the CDRs on each Fab region are also identical. This means a single IgG molecule possesses __
bivalency
This __ allows the molecule to bind two identical epitopes, facilitating the cross-linking of antigens into large immune complexes.
dual chain contributions
The CDRs from both light and heavy chains contribute to binding, though heavy chain usually contributes the most.
antigen cross-linking
since binding sites are identical, antibodies can bridge two separates antigens simultaneously
geometric precision
the specific folding of peptide chain creates a topographical match for the epitope, ensuring high affinity
human IgG4
unlike other substances, __ is dynamic
hybrid antibodies
human IgG4 can exchange regions with other iGg4 molecules to generate __
IgG
highest concentration in blood
IgM
second highest serum concentration (in most mammals)
IgA
Third highest concentration in most mammals. The predominant Ig in secretions such as SALIVA, MILK, & INTESTINAL FLUID
IgD
primarily a BCR, rarely encountered in body fluids
IgE
very low concentration in serum and mediates allergic reactions
spleen, lymph nodes, bone marrow
igg produced by plasma cells in the __
immunoglobulin g
180 kDa
smallest of ig molecules
important in inflammation
secondary lymphoid organs
igm produced by plasma cells in __
B-Cells
Secreted (Blood)
two different forms of igm
immunoglobulin m
Major Ig produced during primary immune response
More efficient than IgG at complement activation, opsonization, neutralizing of virusws, and agglutination.
intestinal tract
respiratory tract
urinary tract
mammary gland
skin
iga present mainly in the __
colostrum, saliva, tears
major immunoglobulin (a) found in __
mucosal surfaces
iga provides local immunity at __ (respiratory and intestinal tracts)
alternative pathway
iga does not activate the classical complement pathway, but can activate the __
phagocytosis and intracellular killing
iga enhances __
coproantibodies
iga known as __ when found in gut contents or feces
serum iga
secretory iga
2 types of IgA
immunoglobulin e
synthesized by plasma cells located beneath body surfaces
reaginic antibody
binds to mast cells and it triggers degranulation and release of inflammatory mediators
type 1 hypersensitivity
ige immediate allergic reaction
parasitic worms
ige provides defense against __
immunoglobulin d
secreted by plasma cells in spleen and lymph nodes
maturation
antigen challenge and binding
clonal selection and proliferation
differentiation
antibody production and secretion
steps on maturation of b cells
any substance that triggers an immune response
antigen = __
epitopes
specific parts of antigens called __
hydrogen and ionic bonds
antigen uses weak forces like __
one antigen
each antibody matches __
high affinity =stronger binding
neutralization
agglutination
precipitation
opsonization
types of reactions of antigens
neutralization
blocks toxins/virus
agglutination
clumps pathogens
precipitation
forms sold complexes
opsonization
enhances phagocytosis
complement system
antibodies activates __
immune cells
antibodies attracts __ and leads to inflammation
protects body from infection
used in vaccines
important in lab tests/diagnostics
importance of antibodies
specific
antigen-antibody binding is __
immune defense
antibody triggers __