variable region

im·mu·no·glob·u·lin (Ig),

(im'yū-nō-glob'yū-lin), One of a class of structurally related proteins, each consisting of two pairs of polypeptide chains, one pair of light (L) low molecular weight chains (κ or λ), and one pair of heavy (H) chains (γ, α, μ, δ, and ε), usually all four linked by disulfide bonds. On the basis of the structural and antigenic properties of the H chains, immunoglobulins are classified (in order of relative amounts present in normal human serum) as IgG (7S in size, 80%), IgA (10-15%), IgM (19S, a pentamer of the basic unit, 5-10%), IgD (less than 0.1%), and IgE (less than 0.01%). All of these classes are homogeneous and susceptible to amino acid sequence analysis. Each class of H chain can associate with either κ or λ L chains. Subclasses of immunoglobulin, based on differences in the H chains, are referred to as IgG1, etc.
When split by papain, IgG yields three pieces: the Fc piece, consisting of the C-terminal portion of the H chains, with no antibody activity but capable of fixing complement, and crystallizable; and two identical Fab pieces, carrying the antigen-binding sites and each consisting of an L chain bound to the remainder of an H chain.
Antibodies are immunoglobulins, and all immunoglobulins probably function as antibodies. However, immunoglobulin refers not only to the usual antibodies, but also to a great number of pathologic proteins classified as myeloma proteins, which appear in multiple myeloma along with Bence Jones proteins, myeloma globulins, and immunoglobulin fragments.
From the amino acid sequences of Bence Jones proteins, it is known that all L chains are divided into a region of variable sequence (V_L) and one of constant sequence (C_L), each comprising about half the length of the L chain. The constant regions of all human L chains of the same type (κ or λ) are identical except for a single amino acid substitution, under genetic controls. H chains are similarly divided, although the V_H region, although similar in length to the V_L region, is only one third or one fourth the length of the C_H region. Binding sites are a combination of V_L and V_H protein regions. The large number of possible combinations of L and H chains make up the "libraries" of antibodies of each individual.

variable region

n. The portion of the amino terminal of an immunoglobulin's heavy and light chains having a variable amino acid sequence.

variable region

The part of an antibody at the tip of each arm (N-terminal region) that varies considerably in its amino acid sequence from one antibody to another. The remaining parts of the structure of antibodies are fixed and almost identical. This region is coded for by the V gene.

variable (V) region

an area of an IMMUNOGLOBIN molecule that is specific to that particular molecule. Compare CONSTANT REGION.

单词	variable region
释义	variable region variable region n. The portion of an immunoglobulin molecule's heavy and light chains that has a variable amino acid sequence and determines the molecule's antigenic specificity. EncyclopediaSeeantibody variable region im·mu·no·glob·u·lin (Ig), (im'yū-nō-glob'yū-lin), One of a class of structurally related proteins, each consisting of two pairs of polypeptide chains, one pair of light (L) low molecular weight chains (κ or λ), and one pair of heavy (H) chains (γ, α, μ, δ, and ε), usually all four linked by disulfide bonds. On the basis of the structural and antigenic properties of the H chains, immunoglobulins are classified (in order of relative amounts present in normal human serum) as IgG (7S in size, 80%), IgA (10-15%), IgM (19S, a pentamer of the basic unit, 5-10%), IgD (less than 0.1%), and IgE (less than 0.01%). All of these classes are homogeneous and susceptible to amino acid sequence analysis. Each class of H chain can associate with either κ or λ L chains. Subclasses of immunoglobulin, based on differences in the H chains, are referred to as IgG1, etc. When split by papain, IgG yields three pieces: the Fc piece, consisting of the C-terminal portion of the H chains, with no antibody activity but capable of fixing complement, and crystallizable; and two identical Fab pieces, carrying the antigen-binding sites and each consisting of an L chain bound to the remainder of an H chain. Antibodies are immunoglobulins, and all immunoglobulins probably function as antibodies. However, immunoglobulin refers not only to the usual antibodies, but also to a great number of pathologic proteins classified as myeloma proteins, which appear in multiple myeloma along with Bence Jones proteins, myeloma globulins, and immunoglobulin fragments. From the amino acid sequences of Bence Jones proteins, it is known that all L chains are divided into a region of variable sequence (V_L) and one of constant sequence (C_L), each comprising about half the length of the L chain. The constant regions of all human L chains of the same type (κ or λ) are identical except for a single amino acid substitution, under genetic controls. H chains are similarly divided, although the V_H region, although similar in length to the V_L region, is only one third or one fourth the length of the C_H region. Binding sites are a combination of V_L and V_H protein regions. The large number of possible combinations of L and H chains make up the "libraries" of antibodies of each individual. variable region n. The portion of the amino terminal of an immunoglobulin's heavy and light chains having a variable amino acid sequence. variable region The part of an antibody at the tip of each arm (N-terminal region) that varies considerably in its amino acid sequence from one antibody to another. The remaining parts of the structure of antibodies are fixed and almost identical. This region is coded for by the V gene. variable (V) region an area of an IMMUNOGLOBIN molecule that is specific to that particular molecule. Compare CONSTANT REGION.
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