The Antibody Problem

Gm, Edelman; Gall, W. Einar

doi:10.1146/annurev.bi.38.070169.002215

Cited by 335 publications

(82 citation statements)

References 80 publications

(132 reference statements)

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“…The smaller fragment is devoid of j3-microglobulin, whereas the 20,000-dalton component formed a complex with this protein. Thus (14,31). To examine if H-2 and HL-A antigens also contain this type of distribution of their intrachain disulfide bonds, papain-solubilized histocompatibility antigens were digested with thermolysin and the resulting domains were isolated.…”

Section: Methodsmentioning

confidence: 99%

Evolutionary relationship between immunoglobulins and transplantation antigens.

Peterson¹,

Rask²,

Sege³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

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The major human and murine histocompatibility antigens are tetrameric molecules with an apparent molecular weight of about 130,000. They are composed of two types of polypeptide chains. The two light chains, previously identified as 6B2-microglobulins, are bound to the two heavy, alloantigenic HL-A or H-2 polypeptide chains by noncovalent interactions only. The heavy chains are held together by disulfide bridge(s) located in the part of the molecule that is attached to the cell membrane.By limited proteolysis of the histocompatibility antigens evidence was obtained suggesting that the heavy chain may consist of three compact domains connected by more extended stretches of polypeptide chain. Each domain appeared to contain a single disulfide bridge encompassing about 60 to 70 amino-acid residues.Staphylococcus aureus protein A is known to bind exclusively to the Fc region of immunoglobulin G. It was, however, observed that protein A interacts in a similar way with the H-2 antigen heavy chain. This observation, together with the homology of the primary structure of ,62-microglobulin to immunoglobulin G, the tetrameric structure of the alloantigens, the organization of the heavy polypeptide chain into compact domains, and the presence of a single, immunoglobulin-like disulfide loop in each domain, establishes a close similarity in structure between histocompatibility antigens and immunoglobulins. The similarity in structural features suggests a common evolutionary origin of the two types of molecules.

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Section: Methodsmentioning

confidence: 99%

Evolutionary relationship between immunoglobulins and transplantation antigens.

Peterson¹,

Rask²,

Sege³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

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“…The precise pairing of two large chromosomes in this manner requires the production of a large number of similar variants of specific protein and RNA molecules that are coded for by recognition genes spaced along the chromosomes. A specific molecule for precise pairing may be analogous to the gamma-globulin molecule (15), which by permutations of a restricted number of amino acids in the variable portion of its peptide chains provides a large number of specific antibodies against antigens.…”

mentioning

confidence: 99%

The Synaptinemal Complex and Four-Strand Crossing Over

Wettstein

1971

Proc. Natl. Acad. Sci. U.S.A.

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“…The most abundant, immunoglobulin-ȍ (IgG), consists of two identical light (L) chains and two identical heavy (H) chains 8 (Fig. 2a).…”

Section: Dna Shuffling In Antibody Formationmentioning

confidence: 99%

The double helix and immunology

Nossal

2003

Nature

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genomic insult. This integrated field is now deciphering the complex regulatory pathways transduced by signalling mechanisms that detect DNA damage and/or arrested DNA replication. As these pathways become better understood, parallel technological gains in gene therapy and therapeutic intervention by rational drug design will offer new strategies for blocking the unwanted consequences of DNA damage, especially cancer.We must remember, however, that while evolution could not have transpired without robust cellular mechanisms to ameliorate the most serious consequences of spontaneous and environmental DNA damage, the process of evolution mandates that the genetic diversification on which Darwinian selection operates be maintained constantly. Thus, life is necessarily a delicate balance between genomic stability and instability -and of mutation and repair. s s

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The Antibody Problem

Cited by 335 publications

References 80 publications

Evolutionary relationship between immunoglobulins and transplantation antigens.

Evolutionary relationship between immunoglobulins and transplantation antigens.

The Synaptinemal Complex and Four-Strand Crossing Over

The double helix and immunology

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