Immunoglobulin Structure: Variation in Amino Acid Sequence and Length of Human Lambda Light Chains

Putnam, Frank W.; Shinoda, Tomotaka; Titani, Koiti; Wikler, Maurice Mosze

doi:10.1126/science.157.3792.1050

Cited by 89 publications

(20 citation statements)

References 17 publications

(4 reference statements)

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“…The ordering of the tryptic peptides was based on their homology to the A-chains VIL [28] and BO [29] and confirmed here for the V-region by the isolation of the chymotryptic overlapping peptides. A detailed description of the methods and results will follow in another publication.…”

Section: Methodssupporting

confidence: 54%

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The primary structure of a monoclonal λ‐type immunoglobulin L‐chain of subgroup II (Bence‐Jones protein NEI): Evolutionary origin of antibody variability

Garver

Hilschmann

1971

FEBS Letters

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Section: Methodssupporting

confidence: 54%

“…On the basis of the amino acid sequence of its variable part the L-chain NE1 clearly belongs to subgroup II of the X-chains, as well as proteins BO [29] and VIL [28] which also contain 216 residues and begin with an N-terminal ar-pyrrolidonecarboxylic acid. As demonstrated in fig.…”

Section: Resultsmentioning

confidence: 99%

The primary structure of a monoclonal λ‐type immunoglobulin L‐chain of subgroup II (Bence‐Jones protein NEI): Evolutionary origin of antibody variability

Garver

Hilschmann

1971

FEBS Letters

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“…However, the size of the proteins within a basic sequence is not always the same. The only known examples in light chains are Mil and Cum in kappa chains and New and Ha in lambda (19,50,65,113). In both cases, the size differences occur around residue 30.…”

Section: An Analysis Of the Type Of Variants Found In V-regionsmentioning

confidence: 97%

The Genetic Basis of Antibody Specificity

Milstein¹,

Munro²

1970

Annu. Rev. Microbiol.

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“…Because of the heterogeneity of the normal immune response, detailed knowledge of the structure of immunoglobulins has been principally derived from the biochemical analyses of the monoclonal immunoglobulins produced in elevated quantities in patients with multiple myeloma, Waldenstrom's macroglobulinemia, and related plasma cell dyscrasias (1)(2)(3). Since the immunoglobulins in these disorders are relatively homogeneous, they are thought to represent a minute fraction of the normal immunoglobulin spectrum each animal has the potential to generate.…”

mentioning

confidence: 99%

Primary structure of a deleted human lambda type immunoglobulin light chain containing carbohydrate: protein Sm lambda.

Garver¹,

Chang²,

Mendicino³

et al. 1975

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

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An internal molecular deletion occurring in a human lambda type immunoglobulin light (L)chain (Sm X) has been defined by sequence analysis. The Sm protein was isolated from the urine of a patient with a plasma cell dyscrasia involving the synthesis of an IgG molecule with both deleted y and X subunits. The Sm A polypeptide chain has an approximate molecular weight of 15,000 and contains 135 amino-acid residues. The constant (C) region is fully intact, comprising 105 residues, whereas the variable region (V) has only 30 residues. The V-region segment represents residues 1 through 30 of normal lambda chains and possesses considerable homology (87%) to lambda chains of subgoup II. Since XI, proteins normally contain 216 amino-acid residues, the defect represents an intramolecular deletion of 81 residues, which is entirely confined to the carboxyterminal three-quarters segment of the V-region, with a resumption of normal synthesis at a glutaminyl residue at position 110, the initiation point of the C-region. Carbohydrate is attached to an Asx residue at position 25, in the first hypervariable region, associated with the sequence triplet Asx-Ser-Ser, which is postulated to be a common recognition site for glycosylation of immunoglobulins. The carbohydrate moiety is a complex oligosaccharide with a branched chain structure containing sialic acid, fucose, mannose, N-acetylglucosamine, and galactose. These structural studies and other findings suggest that restricted areas in the DNA of immunoglobulin genes, such as the hinge regions of heavy (H) and light (L) chains and the hypervariable regions, are particularly susceptible to breakage and reunion. We postulate that the genetic defect of protein Sm could have originated from a somatic mutational event in the plasmacyte precursor during or after the integration of the V and C genes. These studies provide additional support for the hypothesis that two distinct structural genes encode a single immunoglobulin polypeptide chain.Because of the heterogeneity of the normal immune response, detailed knowledge of the structure of immunoglobulins has been principally derived from the biochemical analyses of the monoclonal immunoglobulins produced in elevated quantities in patients with multiple myeloma, Waldenstrom's macroglobulinemia, and related plasma cell dyscrasias (1-3). Since the immunoglobulins in these disorders are relatively homogeneous, they are thought to represent a minute fraction of the normal immunoglobulin spectrum each animal has the potential to generate. One consequence of the extensive data on Bence Jones and myeloma proteins has been to lend credence to the theory advocated by Abbreviations: The nomenclature and abbreviations for immunoglobulins, their subunits, proteolytic fragments and genetic markers are those recommended by the

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Immunoglobulin Structure: Variation in Amino Acid Sequence and Length of Human Lambda Light Chains

Cited by 89 publications

References 17 publications

The primary structure of a monoclonal λ‐type immunoglobulin L‐chain of subgroup II (Bence‐Jones protein NEI): Evolutionary origin of antibody variability

The primary structure of a monoclonal λ‐type immunoglobulin L‐chain of subgroup II (Bence‐Jones protein NEI): Evolutionary origin of antibody variability

The Genetic Basis of Antibody Specificity

Primary structure of a deleted human lambda type immunoglobulin light chain containing carbohydrate: protein Sm lambda.

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