Chemical and Genetic Characterization of a Monoclonal IgA(λ) Protein with Both Cryo‐ and Pyro‐Precipitability

Wang, A. C.; Fudenberg, H. Hugh; Wang, I. Y.; Watanabe, Akiko

doi:10.1111/j.1365-3083.1976.tb00284.x

Cited by 10 publications

(6 citation statements)

References 25 publications

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“…The elution profile of amyloid 758 from Sephadex G-100 column and that of a previously described AAIV amyloid protein 808 [19] resemble each other, showing two major peaks. The second peak containing the major subunit amyloid protein was asymmetric in both instances.…”

Section: Isolation and Antigenic Analysis Of Amyloid Protein 758mentioning

confidence: 60%

“…The amino acid sequence of protein RS showed only six amino acid differences among the first 34 amino acid residues as compared with the prototype AAV protein AR and, furthermore, contained the very typical sequence pattern of the AV subgroup proteins-that is, Asp-Phe-Met at the N-terminus [16]. In addition, strong sequence homologies were seen with other reported AAV proteins [16,19].…”

Section: Discussionmentioning

confidence: 99%

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Further Structural and Antigenic Studies of Light‐chain Amyloid Proteins

Westermark

Sletten

et al. 1981

Scand J Immunol

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The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a V lambda IV Bence-Jones protein and a previously described A lambda IV amyloid protein. The two A lambda IV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-A lambda IV antiserum raised against one or the other of the two proteins. In addition, another new A lambda V amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the A lambda V subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.

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Section: Isolation and Antigenic Analysis Of Amyloid Protein 758mentioning

confidence: 60%

Section: Discussionmentioning

confidence: 99%

Further Structural and Antigenic Studies of Light‐chain Amyloid Proteins

Westermark

Sletten

et al. 1981

Scand J Immunol

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“…Four additional XVI proteins have since been identified from sequence analyses of the light chains isolated from the IgAX protein YAM (11), the IgGX protein KIN (12), the Bence Jones protein NIG-48 (13), and the protein isolated from amyloid fibrils of patient RS (14). Variable region subgroups of human K-and X-light chains have been also identified immunochemically (3,16 V region antigenic determinants when tested with antisera prepared against the alkali-denatured protein AR (14).…”

Section: Discussionmentioning

confidence: 99%

“…The specificity of antiserum R394 was made evident through gel immunodiffusion analysis of a XVI light chain-containing monoclonal immunoglobulin, the IgAX protein YAM (11). Protein YAM and Bence Jones protein GIO formed a precipitin reaction of identity and, as shown in Fig.…”

mentioning

confidence: 99%

Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda).

Solomon¹,

Frangione²,

Franklin³

1982

J. Clin. Invest.

235

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A B S T R A C T An antiserum prepared against a ABence Jones protein from a patient (SUT) who had multiple myeloma and amyloidosis had specificity for X-light chains of the chemically defined variable (V) region X-chain subgroup XVI. Sequence analyses of protein SUT and of five other X-light chains recognized immunologically as of the VAVI subgroup revealed that all six proteins had the N-terminal sequence characteristic for prototype XVI proteins. The isotypic nature of the VAVI subgroup was demonstrated immunochemically: XVI molecules were detected among light chains isolated from the IgG proteins of each of 12 normal individuals and XVI antigenic determinants were also detectable on the intact IgG proteins. The frequency of XVI molecules among X-type light chains is estimated to be -5% based on the finding that 5 of 91 X Bence Jones proteins were of the V,\vI subgroup.Proteins of the VAVI subgroup, in contrast to those of the other five chemically-classified X chain subgroup, appear to be preferentially associated with the amyloid process as evidenced by the fact that all six XVI proteins were obtained from patients with amyloidosis AL and, in addition, 5 of 42 X-type monoclonal immunoglobulins from patients with primary or myelomaassociated amyloidosis were classified by immunodiffusion analyses as having XVI-type light chains.

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“…Three A-light-chain proteins with a N-terminal amino acid sequence very similar to that of protein AR have been reported [JAM (Skinner et al, 1975), YAM (Wang et al, 1976) and RS (Natvig et al, 1980)]. Protein JAM has only been characterized up to residue 16, protein YAM up to residue 22 and protein RS up to residue 34.…”

Section: Vai Vaii Vaiii Vaiv Vavmentioning

confidence: 99%

The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein AR

Sletten¹,

Natvig²,

Husby³

et al. 1981

Biochemical Journal

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The amino acid sequence of an amyloid-fibril protein of immunoglobulin light-chain type (AL) was elucidated. The sequence determination involved digesting the protein with trypsin, thermolysin and pepsin. The protein was found to consist of 154 amino acid residues and is thus missing about half of the constant region of a light chain. A certain heterogeneity in the length of the polypeptide was observed in the C-terminal region. The amino acid sequence from CDR (complementary-determining region) 1 and FR (framework region) 3 indicated an oligoclonal origin of the protein. By comparing the primary structure of protein AR with other lambda- and even kappa-chains, it was revealed that protein AR had an insertion of two residues of aspartic acid, namely residues 68 and 69, which has not been reported previously in light chains. The overall sequence homology in the variable region showed that protein AR is more similar to V lambda V than to the other subgroups [Kabat, Wu & Bilofsky (1979) Variable regions of Immunoglobulin Chains, Medical Computer Systems, Bolt, Beranek and Newman, Cambridge, MA].

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Chemical and Genetic Characterization of a Monoclonal IgA(λ) Protein with Both Cryo‐ and Pyro‐Precipitability

Cited by 10 publications

References 25 publications

Further Structural and Antigenic Studies of Light‐chain Amyloid Proteins

Further Structural and Antigenic Studies of Light‐chain Amyloid Proteins

Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda).

The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein AR

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