Complete Amino Acid Sequence of the Mu Heavy Chain of a Human IgM Immunoglobulin

Putnam, Frank F.W.; Florent, G.; Paul, C.; Shinoda, Tomotaka; Shimizu, Akira

doi:10.1126/science.182.4109.287

Cited by 256 publications

(94 citation statements)

References 30 publications

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“…The IgM in P. sinensis and in other reptiles (Turchin and Hsu, 1996;Deza and Espinel, 2008), as well as in all other classes of vertebrates have all a four constant domain structure, e.g. from fish to mammals a four-constant domain structure has been reported for IgM (Putnam et al, 1973;Dahan et al, 1983;Kokubu et al, 1988;Schwager et al, 1988;Wilson et al, 1990;Turchin and Hsu, 1996). The IgY in P. sinensis as well as in other vertebrates such as in amphibians (Amemiya et al, 1989;Warr et al, 1995) and avians (Zhao et al, 2000;Lundqvist et al, 2001), in which this Ig molecule is found, has also a conserved four constant domain structure.…”

Section: Discussionmentioning

confidence: 94%

IgM, IgD and IgY and their expression pattern in the Chinese soft-shelled turtle Pelodiscus sinensis

Wang

Nie

2009

Molecular Immunology

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Section: Discussionmentioning

confidence: 94%

IgM, IgD and IgY and their expression pattern in the Chinese soft-shelled turtle Pelodiscus sinensis

Wang

Nie

2009

Molecular Immunology

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“…3, there are seven sets of homologous positions. These are: (i) within the CHI domain (a2, A, and e); (ii) just before the hinge [a2 A2m (2) and E]; (iii) within the hinge (GlcN in At and GaIN in al); (iv) just inside the first domain of Fc (04 ih al and a2); (v) 40 residues down the first domain of Fc (yl, ,A, and e); (vi) between the first and second domains of Fc (a2 allotypes); and (vii) 14 residues from the COOH-terminus of the extended chain (al, a2, and A).…”

Section: Resultsmentioning

confidence: 99%

“…With rare exceptions governed by the presence of a signal acceptor tripeptide sequence, the carbohydrate is present only on the heavy chain and is confined to the constant (C) region of the heavy chain. We earlier reported the location and nature of the five oligosaccharides of the At chain of human IgM (1,2). In contrast, the oy chain of human IgG has a single oligosaccharide (3), and the E chain of human IgE is reported to have six (4).…”

mentioning

confidence: 99%

Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins.

Toraño¹,

Tsuzukida²,

Liu³

et al. 1977

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

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The location, number, and kinds of oligosaccharides in human IgAl and IgA2 immunoglobulins have been determined by amino acid sequence analysis of the a heavy chains. Both A2m allotypes of the a2 chain of IgA2 have two GlcN oligosaccharides that are absent in the al chain, but they lack GalN. The A2m(2) allotype has a fifth GlcN oligosaccharide. The a chains of IgA proteins also have subclass-specific and allotype-specific differences in amino acid sequence. Although other classes of human immunoglobulins differ in the number and kind of oligosaccharides, the sites are often homologous and are related to the immunoglobulin domain structure. Evolutionary preservation of the tripeptide acceptor sequence for GlcN probably indicates both a structural and biological role for carbohydrate.Although the five classes of human immunoglobulins differ greatly in their content of carbohydrate and in its distribution along the polypeptide chain, the carbohydrate often is in homologous positions and usually seems to lie in between the compact domains of the heavy chain or on the surface of a domain. With rare exceptions governed by the presence of a signal acceptor tripeptide sequence, the carbohydrate is present only on the heavy chain and is confined to the constant (C) region of the heavy chain. We earlier reported the location and nature of the five oligosaccharides of the At chain of human IgM (1, 2). In contrast, the oy chain of human IgG has a single oligosaccharide (3), and the E chain of human IgE is reported to have six (4). In all these cases the oligosaccharide contains glucosamine (GlcN), which is attached to asparagine by an N-glycosidic linkage. The IgAl subclass is unusual among glycoproteins in having two types of linkage to the polypeptide chain, the N-glycosidic linkage of GlcN to asparagine and an O-glycosidic linkage of galactosamine (GalN) to serine (5, 6). Recently we reported (7) the complete amino acid sequence of a human IgAl immunoglobulin (designated Bur), including the location of five GalN carbohydrates in the hinge region, two GlcN oligosaccharides in the Fc region, and an adventitious GlcN oligosaccharide in the variable (V) region of this al heavy chain. We have now determined the amino acid sequence of the C region of two a2 heavy chains representing different allotypes of the IgA2 subclass, namely, the A2m (2) MATERIALS AND METHODSHuman IgA was prepared from the serum of patients with multiple myeloma who produced large amounts of monoclonal IgA. The procedure involved ammonium sulfate precipitation, ion exchange chromatography, and gel filtration techniques (9, 10). The purity of the IgA was tested by immunodiffusion and immunoelectrophoresis with monospecific antisera and by gel electrophoresis and ultracentrifugation (9, 10). The purified IgA proteins were reduced at room temperature under N2 with 0.01 M dithiothreitol for 1 hr followed by alkylation with iodoacetic acid (10% molar excess) or ethylene imine. The heavy and light chains were separated on a Sephadex G-100 column. The...

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“…The Cys-residue in position 408 has been demonstrated to participate in the /_-y-inter-chain (inter-subunit) --S-Sbond. The residue Gl~x~~~ found in protein BO corresponds to residue Asx~~~ in IgM Ou and Gal sequences [9,10] but it has been found in the intersubunit Cys peptides isolated from IgM He [ 121.…”

Section: Resultsmentioning

confidence: 99%

The inter‐chain disulfide bonds of a μ‐chain disease protein

Mihaesco

1974

FEBS Letters

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Complete Amino Acid Sequence of the Mu Heavy Chain of a Human IgM Immunoglobulin

Cited by 256 publications

References 30 publications

IgM, IgD and IgY and their expression pattern in the Chinese soft-shelled turtle Pelodiscus sinensis

IgM, IgD and IgY and their expression pattern in the Chinese soft-shelled turtle Pelodiscus sinensis

Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins.

The inter‐chain disulfide bonds of a μ‐chain disease protein

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