EurekaMag
+ Translate
+ Most Popular
Advantages and disadvantages of bordeaux mixture and of lime-sulphur used on apples in the growing season
Observations on the Umaria marine bed
10 years of hearing conservation in the Royal Air Force
Chocolate crumb - dairy ingredient for milk chocolate
Effect of daily gelatin ingestion on human scalp hair
Comparison of rice bran and maize bran as feeds for growing and fattening pigs
The composition of pampas-grass (Cortaderia argentea.)
The Accraian Series:
The mechanism of the Liebermann-Burchard reaction of sterols and triterpenes and their esters
Cerebrovascular Doppler ultrasound studies (cv-Doppler)
Toria: PT-303 - first national variety
Hair growth promoting activity of tridax procumbens
Productivity of Pekin x Khaki Campbell ducks
A stable cytosolic expression of VH antibody fragment directed against PVY NIa protein in transgenic potato plant confers partial protection against the virus
Solar treatment of wheat loose smut
Swimmers itch in the Lake of Garda
Bactofugation and the Bactotherm process
The effects of prefrontal lobotomy on aggressive behavior in dogs
Visual rating scales for screening whorl-stage corn for resistance to fall armyworm
Breakdown of seamounts at the trench axis, viewed from gravity anomaly
Kooken; pennsylvania's toughest cave
Recovery of new dinosaur and other fossils from the Early Cretaceous Arundel Clay facies (Potomac Group) of central Maryland, U.S.A
Zubor horny (Bison bonasus) v prirodnych podmienkach Slovensku
The extended Widal test in the diagnosis of fevers due to Salmonella infection
Hair of the american mastodon indicates an adaptation to a semi aquatic habitat

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


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



Proceedings of the National Academy of Sciences of the United States of America 72(11): 4559-4563



ISSN/ISBN: 0027-8424

PMID: 812098

DOI: 10.1073/pnas.72.11.4559

An internal molecular deletion occurring in a human lambda type immunoglobulin light (L)-chain (Sm lambda) 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 gamma and lambda subunits. The Sm lambda 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 subgroup II. Since lambdaII 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 and two distinct structural genes encode a single immunoglobulin polypeptide chain.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 041068912

Download citation: RISBibTeXText

Related references

Human lambda light-chain constant region gene CMor lambda: the primary structure of lambda VI Bence Jones protein Mor. Proceedings of the National Academy of Sciences of the United States of America 82(10): 3415-3419, 1985

V lambda and J lambda-C lambda gene segments of the human immunoglobulin lambda light chain locus are separated by 14 kb and rearrange by a deletion mechanism. European Journal of Immunology 21(6): 1513-1522, 1991

Genomic structure of the human Ig lambda 1 gene suggests that it may be expressed as an Ig lambda 14.1-like protein or as a canonical B cell Ig lambda light chain: implications for Ig lambda gene evolution. Journal of Experimental Medicine 173(2): 305-311, 1991

Genomic structure of the human Ig lambda 1 gene suggests that it may be expressed as an Ig lambda 14.1-like protein or as a canonical B cell Ig lambda light chain: implications for Ig lambda gene evolution. Journal of Experimental Medicine 173(2): 305-311, 1991

Association of human lambda light chain V/J/C segments: serologic analysis and primary structure of the lambda VI Bence Jones protein THO. Journal of Immunology 136(2): 716-719, 1986

The primary structure of a monoclonal human lambda-type immunoglobulin L-chain of subgroup II (Bence-Jones protein NEI). European Journal of Biochemistry 26(1): 10-32, 1972

Localization of the carbohydrate units in a human immunoglobulin light chain, protein Sm lambda. European Journal of Biochemistry 115(3): 643-652, 1981

Human immunoglobulin C lambda 6 gene encodes the Kern+Oz-lambda chain and C lambda 4 and C lambda 5 are pseudogenes. Proceedings of the National Academy of Sciences of the United States of America 84(24): 9074-9078, 1987

Partial amino acid sequence of an amyloid fibril protein from nodular primary cutaneous amyloidosis showing homology to lambda immunoglobulin light chain of variable subgroup III (a lambda III). Journal of Investigative Dermatology 95(3): 301-303, 1990

Rule of antibody structure. Primary structure of a human monoclonal IgAl-immunoglobulin (myeloma protein Tro). VI. Amino acid sequence of the L-chain, lambda-type, subgroup II. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 360(12): 1903-1918, 1979

The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS (immunoglobulin light chain, type lambda). Biological Chemistry Hoppe-Seyler 366(7): 617-625, 1985

Human immunoglobulin kappa light-chain genes are deleted or rearranged in lambda-producing B cells. Nature 290(5805): 368-372, 1981

Primary localized amyloidosis of the eyelid: two cases of immunoglobulin light chain-derived proteins, subtype lambda V respectively lambda VI. Clinical and Experimental Immunology 106(2): 362-366, 1996

Primary structure of a human IgA1 immunoglobulin. V. Amino acid sequence of a human IgA lambda light chain (Bur). Journal of Biological Chemistry 254(18): 9006-9016, 1979

The primary structure of a monoclonal immunoglobulin L-chain of lambda-type, subgroup I (Bence-Jones protein Vor.). Hoppe-Seyler's Zeitschrift für Physiologische Chemie 355(1): 85-88, 1974