Untitled - D Ank Unlimited

antibodies to histidyl t-RNA synthetase (anti-HRS) 45 antibody deficiency syndrome
potential in therapy. Antibodies in the blood serum of any
given animal species may be grouped according to their
physicochemical properties and antigenic characteristics.
Immunoglobulins are not restricted to the plasma but may
be found in other body fluids or tissues such as urine,
spinal fluid, lymph nodes, spleen, etc. Immunoglobulins
do not include the components of the complement system.
Immunoglobulins (antibodies) constitute approximately 1
to 2% of the total serum proteins in health. Gamma globulins
comprise 11.2 to 20.1% of the total serum content in
humans. Antibodies are in the gamma globulin fraction of
serum. Electrophoretically, they are the slowest migrating
fraction.
antibodies to histidyl t-RNA synthetase (anti-HRS)
Antibodies with a formation closely associated with DR3
in Caucasians. DR6 may be increased in African-American
patients with this autoantibody. The supertypic DR specificity
DR52 is found among essentially all individuals with
anti-HRS. This specificity is encoded by the DRB3 gene,
which is present on haplotypes bearing DR3, DR5, or DR6
and is also represented on the DR8 molecule. Essentially all
patients with anti-HRS have one or two of these DR alleles.
All are DR52-positive. The first hypervariable regions
of the DRB1 genes encoding DR3, DR5, DR6, and DR8
have homologous sequences. This homology is believed to
predispose to the development of immune reactivity against
HRS.
antibodies to Mi-1 and Mi-2
Antibodies to Mi-1 and Mi-2 have been found exclusively in
diabetes mellitus (DM) patients (15 to 35%). Anti-Mi-1 has
been found in a small percentage of DM patients but also
in 5% of patients with systemic lupus erythematosus (SLE),
including 7% of those with anti-RNP and 9% of those with
anti-Sm. It has also been shown to bind bovine IgG and is
not helpful in diagnosis.
antibody absorption test
A serological assay based upon the ability of a crossreactive
antigen to diminish a serum sample’s titer of antibodies
against its homologous antigen (i.e., the antigen that
stimulated its production). Crossreactive antibodies and
crossreactive antigens may be detected in this way.
1.
2.
Antigen(x)
Antigen(y)
Antibody(z)
Antibody(z)
Antibody affinity.
antibody affinity
The force of binding of one antibody molecule’s paratope
with its homologous epitope on the antigen molecule. It is
a consequence of positive and negative portions affecting
these molecular interactions.
antibody–antigen intermolecular forces
The various types of bonds that participate in the specific
interaction between antibody and antigen molecules
are relatively weak physical forces. They fall into three
classes: (1) van der Waals or electrodynamic forces,
(2) hydrogen bonding or polar forces, and (3) electrostatic
forces. Covalent bonds are not involved in antibody–antigen
interactions.
antibody-binding site
The antigen-binding site of an antibody molecule, known
as a paratope and comprised of heavy chain and light
chain variable regions. The paratope represents the site of
attachment of an epitope to the antibody molecule. The
complementarity-determining hypervariable regions play
a significant role in dictating the combining site structure
together with the participation of framework region residues.
The T cell receptor also has antigen-binding sites in
the variable regions of its α and β (or γ and δ) chains.
antibody deficiency syndrome
A few patients have been observed in which normal immunoglobulin
levels are present, but the ability to mount an
immune response to immunogenic challenge is impaired.
This condition is associated with several separate disease
states and might more properly be considered a syndrome.
Repulsive forces
Antigen epitope
High attraction High repulsion
Antibody affinity.
Forces of attraction
(only over very short distances)
A