Membrane Immunoglobulins of Vertebrate Lymphocytes

Warr, Gregory W.

doi:10.1007/978-1-4615-9131-3_6

Cited by 8 publications

(1 citation statement)

References 137 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Immunoglobulin-like molecules also occur as membrane-bound receptors on the surface of bonemarrow derived B-lymphocytes. Recognition of the corresponding antigen leads to proliferation and antibody secretion (for reviews see: [3][4][5]). …”

Section: Schliisselw6rtermentioning

confidence: 99%

Die r�umliche Struktur der Immunglobulin-Molek�le

Huber

1980

Klin Wochenschr

View full text Add to dashboard Cite

Immunoglobulin molecules of the class G (antibody molecules) consist of two heavy chains (50,000 dalton molecular weight) and two light chains (25,000 dalton). The overall shape is a Y with the arms formed by the light chains and the N-terminal half of the heavy chains in tight association. The stem is formed by the C-terminal halves of the heavy chains. The heavy and the light chains fold into globular domains of molecular weights of 12,000 dalton. There are four domains of the heavy chain and two of the light chain. All these domains show a similar fold, consisting of two B-sheets but display considerable differences in detail. The N-terminal variable domains of heavy and light chains and specifically the hypervariable polypeptide segments of the domains, located at the tips of the Y, constitute the antigen and hapten binding site. The nature of the amino acid residues of the hypervariable loops determines the shape and the specificity of the antibody. All domains pair tightly laterally, except the CH2 domains of the heavy chain. This domain has carbohydrate bound which prevents lateral association. Longitudinal interaction between the domains is loose and allows flexibility in the arrangement. Flexibility is probably of significance for antibody function. Arm (Fab) and stem (Fc) parts are linked by the hinge peptide which contains a segment with a unique conformation of two parallel poly-proline helices. Antigen binding triggers effector functions of antibodies. Antigen binding is at the tips of the Y-shaped antibody, but effector functions are displayed by the stem part. It is an open question whether conformational changes of the antibody molecule play a significant role in the trigger mechanism.

show abstract

Section: Schliisselw6rtermentioning

confidence: 99%

Die r�umliche Struktur der Immunglobulin-Molek�le

Huber

1980

Klin Wochenschr

View full text Add to dashboard Cite

show abstract

Lymphocyte heterogeneity in the trout, Salmo gairdneri, defined with monoclonal antibodies to IgM

1983

Self Cite

View full text Add to dashboard Cite

A monoclonal antibody to trout serum IgM was tested by immunofluorescence analysis with lymphocytes from thymus, spleen and head kidney. By visual examination, the antibody reacted with only a subpopulation of lymphocytes. The mean values +/- SE for positive cells were 5.2 +/- 2.3% in the thymus, 30.3 +/- 7.9% in the spleen and 12.4 +/- 3.0% in the head kidney. Flow cytofluorometric analysis revealed evidence of heterogeneity by size among the membrane IgM-positive cells of the head kidney and spleen. Depletion of head kidney cells positive for surface IgM by an immune affinity adherence technique of panning, using monoclonal anti-IgM, significantly reduced the mitogenic response to lipopolysaccharide but not to concanavalin A. It is suggested that this information supports the existence of distinct subpopulations of fish lymphocytes that may be homologous in certain respects to mammalian T and B type cells.

show abstract

Immunologic Relations Among Fish Groups

Rijkers

1985

Evolutionary Biology of Primitive Fishes

View full text Add to dashboard Cite

Membrane Immunoglobulins of Vertebrate Lymphocytes

Cited by 8 publications

References 137 publications

Die r�umliche Struktur der Immunglobulin-Molek�le

Die r�umliche Struktur der Immunglobulin-Molek�le

Lymphocyte heterogeneity in the trout, Salmo gairdneri, defined with monoclonal antibodies to IgM

Immunologic Relations Among Fish Groups

Contact Info

Product

Resources

About