Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myeloma protein Nie has been isolated from the serum of a myeloma patient by free flow continuous high voltage electrophoresis or by Pevicon-block electrophoresis. It was further purified by ion-exchange chromatography and gel filtration, and characterized by amino acid analysis and end group determination. Serologically, the protein belongs to the IgG1 subclass. It has been typed as Gm1+, 2-,4- and 17+. The L-chain is of the k-type. The L- and H-chains have been separated by gel-filtration after partial reduction and alkylation and characterized by amino acid analysis and end group determination. The F(ab)- and Fc-fragments, prepared by limited tryptic digestion, have been separated and characterized. Cyanogen bromide splitting products have been prepared both from the intact IgG and from the Fc-and the partially reduced and alkylated F(ab)-fragment. These splitting products have been purified and characterized by amino acid analysis and end group determination. By means of these cyanogen bromide splitting products and by partial reduction and alkylation, the disulfide bridges in the protein could be localized: one L-H-bridge, two inter-H-bridges and four loop forming intra-H-bridges.
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PMID:[Rule of antibody structure. the primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), I: Purification and characterization of the protein, the L- and H-chains, the cyanogenbromide cleavage products, and the disulfide bridges (author's transl)]. 100 29

The heavy chain of a human myeloma protein (Vin) belonging to the gamma4 subclass was subjected to tryptic digestion after reduction and carboxymethylation. Cyanogen bromide fragments were also prepared and all 19 tryptic peptides that account for one of them (the Fc-like fragment) were studied. Selected peptic peptides were isolated and provided evidence for the order of 15 of the tryptic peptides. In addition the sequence of two large peptic peptides derived from two sections of the molecule including all the interchain bridges is presented. Comparison with published data on other chains allows us to propose a sequence of gamma4 chains that extends from just before the presumed starting point of the invariable region (at about residue 113) to the C-terminal end of the chain (approx. residue 446), except for a section of about 50 residues. The results of the comparison suggest that the immunoglobulin subclasses have a recent independent evolutionary origin in different species. Implications for complement fixation and for the evolutionary origin of antibody diversity are also discussed.
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PMID:Human immunoglobulin subclasses. Partial amino acid sequence of the constant region of a gamma 4 chain. 419 99

Cyanogen bromide cleavage of the heavy (alpha) chain of protein 315 (an immunoglobulin A mouse myeloma protein with anti-dinitrophenyl activity) yielded five fragments of which one (CN2), with 156 residues, contained the chain's entire variable region. Determination of the amino-acid sequence of CN2 showed that: (1) the variable region has appreciable homology (about 33% identities) with the variable region of the light chain from the same molecule; and (2) the constant-region sequence immediately following the probable transition from variable to constant domains is the same in the protein-315 alpha as in human gamma1 and mu chains (-Val-Ser-Ser-). The sequence of the cyanogen bromide octapeptide (CN5) from the carboxy terminus of the protein-315 heavy chain closely resembles the corresponding segments of human alpha and mu chains.
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PMID:Amino-acid sequence of the variable region of the heavy (alpha) chain of a mouse myeloma protein with anti-hapten activity. 452 22

Unlike IgA and IgM, IgG has not yet been shown to form covalent polymers. However in the presence of specific Ag, murine IgG3 has been shown to polymerize through noncovalent interactions. In contrast to the noncovalent oligomers found with murine IgG3, we have detected covalent dimers in three different recombinant human IgG2 Abs produced in myeloma cells. Both IgG2,kappa and IgG2,lambda can form dimers. In addition, analysis of pooled human gamma globulin and several normal sera revealed the presence of IgG2 dimers. The IgG2 dimers are in contrast to the noncovalent IgG dimers found in pooled sera of multiple donors resulting from idiotype/anti-idiotype (Id/anti-Id) interactions. Cyanogen bromide cleavage analysis suggests that one or more Cys residues in the gamma 2 hinge are involved in dimer assembly. The potential role of IgG2 dimers in immunity against carbohydrate Ags is discussed.
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PMID:Human IgG2 can form covalent dimers. 1262 70