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Untitled - D Ank Unlimited

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Fab′′ fragment 262 factor H<br />

The Fab fragment is composed of one light chain and the variable and C H1 regions of a heavy chain. They are united by disulfide bonds and have a single<br />

binding site for antigen. The heavy chain part of a Fab fragment is referred to as Fd. Further digestion with papain yields an Fc′.<br />

s<br />

s<br />

s<br />

s<br />

s<br />

s<br />

s s<br />

Pepsin<br />

digestion<br />

F(ab′) 2 fragment<br />

A product of pepsin digestion of an immunoglobulin G<br />

(IgG) molecule. This 95-kDa immunoglobulin fragment<br />

has a valence or antigen-binding capacity of two that<br />

renders it capable of inducing aggulination or precipitation<br />

with homologous antigen. However, the functions associated<br />

with the Fc region of the intact IgG molecule, such<br />

as complement fixation and attachment to Fc receptors on<br />

cell surfaces, are missing. Pepsin digestion occurs on the<br />

carboxyl terminal side of the central disulfide bond at the<br />

hinge region of the molecule which leaves the central disulfide<br />

bond intact. The C H2 domain is converted to minute<br />

peptides, yet the C H3 domain is left whole, and the two C H3<br />

domains comprise the pFc′ fragment.<br />

Fab′′ fragment<br />

Refer to F(ab′) 2 fragment.<br />

Fabc fragment<br />

A 5-S intermediate fragment produced by partial digestion<br />

of immunoglobulin G (IgG) by papain in which only<br />

one Fab fragment is cleaved from the parent molecule in<br />

the hinge region. This leaves the Fabc fragment, which is<br />

composed of a Fab region bound covalently to an Fc region<br />

and is functionally univalent.<br />

Facb fragment<br />

Abbreviation for fragment antigen and complement binding.<br />

The action of plasmin on immunoglobulin G (IgG) molecules<br />

denatured by acid cleaves C H3 domains from both heavy chain<br />

Fd´<br />

F(ab´) 2<br />

F(ab′) 2 fragment containing 2 Fd′ heavy chain portions.<br />

s s<br />

s<br />

s<br />

s<br />

s s<br />

ss ss<br />

Pepsin<br />

digestion<br />

s<br />

s<br />

s s<br />

F(ab´) 2<br />

Reduction<br />

Pepsin digestion of an IgG molecule leading to formation of F(ab′) 2 intermediate fragments with reduction to the formation of Fab′ fragments.<br />

Fab´<br />

s s<br />

Fab´<br />

constituents of the Fc region. This yields a bivalent fragment<br />

functionally capable of precipitation and agglutination with an<br />

Fc remnant still capable of fixing complement.<br />

FACS ®<br />

Refer to fluorescence-activated cell sorter.<br />

factor B<br />

An alternative complement pathway component. It is a<br />

739-amino-acid residue, single-polypeptide chain that<br />

combines with C3b and is cleaved by factor D to produce<br />

alternative pathway C3 convertase. Cleavage by factor D is<br />

at an arginine–lysine bond at position 234 to 235 to yield<br />

an amino terminal fragment Ba. The carboxyl-terminal<br />

fragment termed Bb remains attached to C3b. C3bBb is C3<br />

convertase, and C3bBb3b is C5 convertase of the alternative<br />

complement pathway. The Bb fragment is the enzyme’s<br />

active site. Factor B has three short homologous, 60-amino<br />

acid residue repeats and four attachment sites for N-linked<br />

oligosaccharides. Alleles for human factor B include BfS<br />

and BfF. The factor B gene is located in the major histocompatibility<br />

complex (MHC) situated on the short arm of<br />

chromosome 6 in humans and on chromosome 17 in mice.<br />

Also called C3 proactivator.<br />

factor D<br />

An alternative complement activation pathway serine<br />

esterase. It splits factor B to produce Ba and Bb fragments.<br />

It is also called C3 activator convertase.<br />

factor D deficiency<br />

An extremely rare genetic deficiency of factor D which has<br />

an X-linked or autosomal-recessive pattern of inheritance.<br />

The sera of affected patients contain only 1% of the physiologic<br />

amounts of factor D, which renders them susceptible to<br />

repeated infection by Neisseria microorganisms. The sera of<br />

heterozygotes contain half the physiologic levels of factor D,<br />

but they have no clinical symptoms related to this deficiency.<br />

factor H<br />

A regulator of complement in the blood under physiologic<br />

conditions. Factor H is a glycoprotein in serum that unites<br />

s s

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