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

A series of seven BALB/c myeloma proteins has been identified with binding specificity for antigens containing beta(1 leads to 6)-D-galactopyranosyl moieties. We have determined the primary amino acid sequence of the first 108 residues from the light chains of three of these proteins. The framework portions of the variable regions of these three light chains are identical with residue 100 at which position three different amino acids are found in the three chains. An additional interchange was found at position 106 in one of the proteins. Based on recent DNA sequence studies suggesting that the variable region ends at residue 97, these substitutions indicate the possible existance of multiple genes coding for the region beginning at residue 98 and continuing toward the carboxy terminus. A single amino acid interchange was observed in complementarity determining regions occurring in L3. This substitution (Ile-Trp) would require changes in all three codon bases to produce the respective amino acids if one were derived from the other. Two of these chains are thus indistinguishable for their first 100 amino acids and are the first pair of k chains to exhibit complete identity over their variable regions.
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PMID:k Chain variable regions from three galactan binding myeloma proteins. 10 73

The discovery of T601, a new mouse-myeloma immunoglobulin A having specificity for beta-D-(1 yields 6)-linked D-galactopyranosyl residues, brings the total number of known antigalactan immunoglobulins to seven. The interaction of T601 with a number of ligands has been investigated. For those ligands showing interaction with the immunoglobulin, the affinity constants have been quantitatively measured by tryptophanyl fluorescence. The values show that protein T601 behaves very similarly to protein X24.
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PMID:A new, mouse-myeloma immunoglobulin A having specificity for beta-D-(1 yields 6)-linked D-galactopyranosyl residues. 80 90

The preparation, properties, and some applications of ferritin conjugates of two plant agglutinins, concanavalin A and Ricinus communis agglutinin, are reported. These conjugates serve as specific electron-dense stains for cell- and membrane-bound saccharide residues of the alpha-D-mannopyranosyl and beta-D-galactopyranosyl configurations, respectively, and as examples of a wide range of ferritin-plant agglutinin conjugates useful as high resolution saccharide stains. By using a technique for preparing flattened membrane specimens, it was found with a variety of mammalian cell plasma membranes (lymphocyte, lymphoma, and myeloma and normal, spontaneously and virally transformed fibroblasts) that the ferritin conjugates were localized exclusively to the exterior face of the membrane, with essentially none found on the cytoplasmic face. On the exterior face the topographical distribution of ferritin conjugates appeared to be random. The asymmetrical distribution of saccharide residues to the outer membrane face can be explained by an "assembly line" process whereby new plasma membrane is made from intracellular precursor membranes. It also suggests that the saccharide-containing components of the plasma membrane do not rotate at any appreciable rate from one membrane surface to the other.
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PMID:The distribution and asymmetry of mammalian cell surface saccharides utilizing ferritin-conjugated plant agglutinins as specific saccharide stains. 412 77

Interactions of polymeric McPC 870 and MOPC 384 mouse IgA myeloma proteins with a streptococcal cell wall tetraheteroglycan (T4-antigen), Salmonella tranoroa lipopolysaccharide (LPS), S. telaviv LPS and its lipid A free polysaccharide were examined by the quantitative precipitin method. Hapten inhibition of myeloma protein precipitation by T4-antigen or S. telaviv LPS indicates a complex anticarbohydrate specificity for 870 and 384 protein combining sites involving several sugars. While the combining site of 870 protein appears to bind alpha-D-mannopyranosyl, alpha-D-galactopyranosyl and alpha-D-glucopyranosyl residues, the combining site of 384 protein can accommodate both the alpha (1----2)-linked glucobiose (kojibiose) and alpha-D-galactopyranosyl but not the alpha-D-mannopyranosyl structure.
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PMID:Interaction of a streptococcal cell wall tetraheteroglycan and Salmonella telaviv lipopolysaccharide with polymeric McPC 870 and MOPC 384 mouse IgA myeloma proteins. 644 9