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The amino acid sequences of the Fd fragments of two human gamma-1 heavy chains

Elizabeth M. Press, +1 more
- 01 May 1970 - 
- Vol. 117, Iss: 4, pp 641-660
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TLDR
The amino acid sequences of the Fd fragments of two human pathological Immunoglobulins of the immunoglobulin G1 class are reported and it is shown that the heavy-chain variable regions are similar in length to those of the light chains.
Abstract
The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another gamma 1 chain, Eu, a mu chain, Ou, and the partial sequence of a fourth gamma 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the gamma 1 chains, Cor.

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Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution

TL;DR: The structure of the Fab' fragment of a human myeloma immunoglobulin was determined by x-ray crystallographic analysis at 2.8-A resolution and the Fourier map of the electron density was correlated with the aminoacid sequence to obtain a three-dimensional model.
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Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains.

TL;DR: These conclusions, however, do not account for antibody complementarity nor do they localize the combining site to any specific portions of the variable region.
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Complete Amino Acid Sequence of the Mu Heavy Chain of a Human IgM Immunoglobulin

TL;DR: The homology of the constant regions of immunoglobulin �, γ, α, and ε heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain.
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Hypervariable regions, idiotypy, and the antibody-combining site.

TL;DR: The most detailed view of the molecular orientation of the immunoglobulin V region, which is consistent with the known serological and immunochemical data is obtained by X-ray diffraction analyses.
Journal ArticleDOI

Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation.

TL;DR: The data show that the carbohydrate plays no direct role in determining the antigenic specificity of HLA antigens, and suggests that HLA heavy chains are structurally related to immunoglobulins and made up of structural homology units.
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