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Untitled - D Ank Unlimited

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pepsinogen antibodies 564 peptidoglycolipid<br />

one F(ab′) 2 fragment, which is bivalent and may manifest<br />

many of the same antibody characteristics as intact IgG<br />

molecules, such as antitoxic activity in neutralizing bacterial<br />

toxins. Cleaving the Fc region from an IgG molecule<br />

deprives it of its ability to fix complement and bind to Fc<br />

receptors on cell surfaces. Pepsin digestion is useful in<br />

diminishing the immunogenicity of antitoxins. It converts<br />

them to F(ab′) 2 fragments that retain antitoxin activity.<br />

pepsinogen antibodies<br />

Antibodies against pepsinogen, which is produced by chief<br />

cells and mucous neck cells. Autoantibodies against pepsinogen<br />

develop in patients with autoimmune atrophic gastritis<br />

with pernicious anemia. Three fourths of patients with<br />

peptic ulcers have pepsinogen antibodies. Autoantibodies<br />

are present in half of patients with pernicious anemia and a<br />

quarter of patients with active duodenal ulcer.<br />

peptide-binding cleft<br />

Part of a major histocompatibility molecule that binds<br />

peptides for display to T lymphocytes. Paired α helices on<br />

a floor of an eight-stranded β-pleated sheet comprise the<br />

cleft. Situated in and around this cleft are polymorphic<br />

residues that are the amino acids that differ among various<br />

MHC alleles.<br />

peptide-binding motif<br />

The assemblage of anchor residues of an MHC isoform<br />

that are common to the peptide amino acid sequences that<br />

interact with the isoform.<br />

peptide interception<br />

A possible cross presentation mechanism. An MHC class<br />

II compartment holding exogenous peptides combines with<br />

a vesicle-harboring MHC class I recycling from the cell<br />

surface. A reduced pH in the MHC class II compartment<br />

causes release of the endogenous peptide from the recycling<br />

MHC class I molecule groove and permits loading of an<br />

exogenous MHC class II compartment peptide, independent<br />

of TAP, onto MHC class I.<br />

peptide map<br />

A fingerprint of peptides in two dimensions prepared by<br />

digestion of a protein with an enzyme such as pepsin. Thin<br />

layer chromatography in one direction and electrophoresis<br />

Glc NAc<br />

HO<br />

CH 2 OH<br />

OH<br />

O<br />

NAc<br />

H<br />

O<br />

CH 3 C - CO<br />

H<br />

O<br />

in the other direction at pH 6.5 yield the fingerprint<br />

pattern.<br />

peptide regurgitation<br />

A possible mechanism of cross presentation. Following<br />

internalization of extracellular proteins and processing<br />

into peptides within dendritic cell endosomes, the<br />

peptides are set free or “regurgitated” back into the<br />

extracellular environment. The extracellular exogenous<br />

peptide may negotiate an exchange of peptides at the cell<br />

surface without intracellular processing. The exogenous<br />

peptide displaces MHC-associated peptides displayed on<br />

the surface.<br />

peptidergic endothelium-derived contrasting factor (EDCF)<br />

A unique 21-amino acid peptide with two intrachain disulfide<br />

bonds. It is homologous to surafotoxin S6b. Also called<br />

endothelin (ET). Four isoforms of ET and two ET receptor<br />

subtypes have been described.<br />

peptide T<br />

A small HIV-1 envelope polypeptide initially believed to<br />

have potential in treating AIDS, but later withdrawn.<br />

peptide vaccine<br />

An immunizing preparation comprised of a small antigenic<br />

peptide capable of generating an immune response.<br />

peptidoglycan layer<br />

Humans have innate immunity against extracellular bacteria.<br />

Neutrophil (PMN), monocyte, and tissue macrophage phagocytosis<br />

leads to rapid microbicidal action against ingested<br />

microbes from the extracellular environment. The capacity<br />

of a microorganism to resist phagocytosis and digestion<br />

in phagocytic cells is a principal feature of its virulence.<br />

Complement activation represents a significant mechanism<br />

for ridding the body of invading microorganisms. A peptidoglycan<br />

layer in the cell walls of Gram-positive bacteria and<br />

lipopolysaccharide (LPS) in the cell walls of Gram-negative<br />

bacteria are able to activate the alternative pathway of<br />

complement without antibody. Also associated with LPS are<br />

flagellar antigen and somatic antigen.<br />

peptidoglycolipid<br />

A part of the wax D fraction extracted from mycobacteria<br />

that contains the adjuvant principle in Freund’s adjuvant.<br />

CH 2OH<br />

CH 3<br />

O<br />

NCOCH 2 OH<br />

H<br />

L-Ala<br />

OH<br />

NHCHCO-NHCHCONH 2<br />

Peptidoglycan (murein).<br />

MA<br />

CH 2<br />

CH 2<br />

D-Glu<br />

CO-NHCH-CO-NHCHCOOH<br />

CH 2<br />

CH 2<br />

CH 2<br />

R-H N-C-CONH 2<br />

H<br />

MDP<br />

D-Ala<br />

CH 3<br />

Meso-DAP

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