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)

Hybridomas secreting monoclonal antibodies to aldosterone were obtained by fusion of myeloma cells and spleen cells from Balb/c mice immunized with aldosterone-3-carboxylmethyloxime-bovine serum albumin. A monoclonal antibody was purified from ascites fluid and characterized. An affinity constant of 1.61 x 10(9) M-1 has been measured and no cross-reactivity with tetrahydroaldosterone (THA), cortisol, cortisone, corticosterone, deoxycorticosterone (DOC), dehydroepiandrosterone (DHA), progesterone and estrone, could be detected. A peroxidase conjugated-antibody (1.5 mole of enzyme per mole of antibody) was obtained and used for microwell enzyme immunoassay and Immun-Blot assay. The high affinity and specificity of this antibody should make the direct determination of aldosterone in biological fluids possible at concentrations as low as 5 x 10(-10) M.
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PMID:Murine monoclonal antibody against aldosterone: production, characterization and use for enzymoimmunoassay. 331 48

The synthetic peptide 166-174 of hCS sequence, corresponding to an antigenic determinant of the protein, was used to elicit MAbs to the native hCS molecule. The synthetic peptide was administered according to different immunization protocols to BALB/c mice, both in the free form or conjugated to carrier proteins. Spleens and popliteal lymph nodes from primed mice were fused with a myeloma cell line to produce MAbs, and selected clones were characterized for isotype and affinity. Spleen fusions gave rise to IgM MAbs, whereas lymph node fusions gave preferentially IgG MAbs. No correlation was found between antibody class and affinity since affinity is highly increased by carrier-conjugation, while it did not enhance IgG production. The free synthetic peptide showed a low immunogenicity: affinities of MAbs produced ranged from 10(5) to 10(7) l/mole, an average 1000-fold lower than the values obtained with carrier-conjugated peptide. In one case, however, carrier conjugation did not give rise to anti-hCS MAbs. Overall, these studies provide a rational approach to the production of anti-protein MAbs by synthetic peptide immunization and offer the opportunity to obtain MAbs of the desired isotype and affinity.
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PMID:Immunogenicity of a free synthetic peptide: carrier-conjugation enhances antibody affinity for the native protein. 361 16

To analyze the humoral immune response to melanoma, human-mouse hybridomas were generated by the fusions of regional lymph node lymphocytes of patients with the mouse myeloma cell line M5. Six stable hybridomas were cloned from six separate lymphocyte parents obtained from three patients. Ascites were obtained from nude mice after i.p. injection with cultured hybridoma cells. The monoclonal antibodies, four immunoglobulin Gs and two pentameric immunoglobulin Ms, were partially purified to remove mouse immunoglobulin and then conjugated to biotin for immunocytochemical and immunohistochemical studies. With the avidin:biotin:peroxidase complex method to detect and amplify binding by the biotin-conjugated human monoclonal antibodies, we found the six antibodies to be reactive against cytoplasmic determinants in five short-term melanoma cultures and formalin-fixed paraffin-embedded melanoma tumors from four patients. The antigenic target of the antibodies identified was not carcinoembryonic antigen. Two antibodies, 2-139-1 and 6-26-3, were studied in more detail. Each stained 25 of 25 specimens of melanomas. Little or no reactivity was detected against fixed sections of normal skin, which included tissues such as epidermis, dermis, monocytes, lymphocytes, and vascular endothelium. More striking was the absence of binding to melanocytes in the basal layer of the skin or to pigmented nevus cells. Both antibodies showed cross-reactivity against other tumors, in particular colonic and prostatic carcinomas. In the normal colon, reactivity was restricted to the surface of the columnar epithelium; no reactivity was detected against normal prostatic epithelium. Reactivity was also not observed against liver and lung. However, the epithelia of the renal tubules, pancreatic ducts, and salivary ducts were all reactive. These human monoclonal antibodies identify cytoplasmic melanoma-associated tumor antigens that appear different from the membrane antigens defined by serological approaches and by most mouse monoclonal antibodies.
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PMID:Human monoclonal antibodies directed against melanoma tumor-associated antigens. 369 90

Mouse hybrid cell clones secreting antigonadotropin releasing hormone monoclonal antibody were developed by fusion of SP2/O-Ag 1.4 myeloma cells with splenocytes of mouse immunized with gonadotropin releasing hormone (GnRH) tagged to tetanus toxoid. The product of hybrid cell clones obtained as ascites fluid from mouse peritoneal cavity had a titre of 10(6) (30-40% binding of 125I-GnRH) in radioimmunoassay. The antibody was IgG2a and Kappa. The association constant (Ka) of the product of hybrid cell clone P(8)16(62) for binding with GnRH was 1.2 X 10(9) L/mole. The monoclonal antibody (P(8)16(62)) was highly specific for the native GnRH and devoid of reactivity with thyroid releasing hormone as tested in competitive radioimmunoassay. The recognition for GnRH agonists by monoclonal was 387-fold less with D-Ser (But)6 des Gly10 GnRH ethylamide and 608-fold less with Bz1-His6 GnRH. Monoclonal anti-GnRH antibody was competent to neutralize the in vivo bioactivity of the hormone as evident by the block of estrus cycle and termination of pregnancy in mice. Termination of pregnancy in animals receiving anti-GnRH monoclonal could be prevented by administration of progesterone.
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PMID:Characteristics and bioefficacy of monoclonal antigonadotropin releasing hormone antibody. 388 52

Three monoclonal antiidiotypic antibodies (AIA) to MOPC 315 IgA, G3 (IgG2b), A2 (IgG1) and D10 (a hybrid molecule consisting of gamma 1 and gamma 2a heavy chains), were characterized with respect to their binding constants (Ka) to MOPC 315 mouse myeloma cells. The Ka of G3 and A2 was 10(8)/mole; and that of D10 was 3 X 10(7)/mole. The AIA did not bind to a non-immunoglobulin (Ig) producing subclone of MOPC 315 cells (MOPC 315.36). Immunotoxins derived by conjugating ricin A chain (RTA) to G3 and A2 but not to D10 preferentially inhibited protein synthesis in MOPC 315 over MOPC 315.36 cells. These results suggest that the effectiveness of these immunotoxins assessed on the basis of their targeted cytotoxicity against MOPC 315 cells was dependent on the Ka but not on the Ig subclass of the AIA component of the immunotoxin.
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PMID:Inhibition of protein synthesis by monoclonal anti-idiotypic antibody-ricin A chain conjugates in MOPC 315 myeloma cells. 403 40

A new subclass of mouse IgG for which we propose the name IgG3 has been shown to have a mol wt of 150,000 consistent with an L(2)H(2) structure, and is present in normal mouse serum at a concentration of 0.1-0.2 mg/ml. Its molecular weight, low carbohydrate content, glycopeptide analysis, and C-terminal analysis are all typical of the IgG class. The intact protein had a strong tendency to form noncovalent aggregates with itself which were dissociable in acid. Upon papain digestion an Fab fragment of 47,000 mole wt was generated along with an Fc fragment which was insoluble at neutral pH. As for its biology, the protein did not fix complement, was not cytophilic for gammaG2 receptor sites on macrophages, and did not show passive cutaneous anaphylaxis. It was very efficiently transported across the placenta so that its concentration in the newborn was twice that in the serum of the mother, compared to the concentration of IgG1 and IgG2 proteins which were only present at one-third the concentration of that found in the serum of the mother. The Fc fragment of this protein reacted with and was solubilized by the staphylococcal A protein which also precipitated the intact immunoglobulin. In addition, the myeloma protein which was the prototype for this gammaG subclass exhibited binding activity for levan which was localized to the Fab fragment.
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PMID:A new mouse immunoglobulin: IgG3. 513 63

A 24-amino acid residue peptide has been isolated from the Fc region of a human IgG1 myeloma protein. The peptide has associated with it the same ability to induce murine B cells to polyclonally secrete antibody as does the intact Fc fragment. Amino acid composition of the peptide indicates that on a mole/mole basis the isolated peptide is identical to that published for residues 335-358 in the Eu IgG1 sequence. This peptide corresponds roughly to the first 24 amino acids of the CH3 domain. It is believed that the immunoregulatory properties that have been ascribed to the Fc fragment are associated with this peptide.
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PMID:Isolation and identification of a biologically active peptide derived from the CH3 domain of human IgG1. 621 50

MOPC 315 mouse myeloma cells which produce an IgA (alpha, lambda 2) with dinitrophenol (DNP)-binding capacity were incubated with a [125I]-labeled monoclonal anti-idiotypic antibody (AIA) (D10) to MOPC 315 IgA. AIA D10 bound specifically to the surface of MOPC 315 cells (binding constant 3.0 X 10(7)/mole) but not to cells of a derivative clone which did not produce IgA. Following binding, D10 was taken up intracellularly and localized in a subcellular fraction which sedimented in a Percoll gradient on the light side of the main lysosomal peak. These results indicate that monoclonal AIA to MOPC 315 IgA is selectively bound and internalized by MOPC 315 myeloma cells.
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PMID:Cellular handling of a monoclonal anti-idiotypic antibody in IgA-producing MOPC 315 mouse myeloma cells. 633 99

Splenocytes from BALB/c mice immunized with a gentamicin-hemocyanin conjugate were fused with X63-Ag8.653 murine myeloma cells to produce hybridomas that secreted monoclonal antibody to gentamicin. Sixteen positive clones were obtained. The monoclonal antibody chosen for a gentamicin immunoassay has been characterized with respect to class, subclass, type of light chain, electrophoretic homogeneity, and binding affinity. Gentamicin monoclonal antibody purified from mouse ascites fluid was analyzed by immunoelectrophoresis, double immunodiffusion, enzyme-linked immunosorbent assay (ELISA), and polyacrylamide gel electrophoresis (PAGE). The results show that the antibody is an IgG2a (kappa). Two bands were detected when the purified antibody was electrophoresed on polyacrylamide gels: a major band and a less mobile minor component (5.6% of the major band). Both were IgG2a (kappa). The major band contained antibody which bound 2.1 moles of the substrate-labeled gentamicin derivative, beta-galactosyl-umbelliferone sisomicin, per mole of IgG, whereas one mole of the minor band bound only 0.095 moles of the substrate-labeled conjugate. The antibody has an affinity constant of 1.22 X 10(10) M-1.
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PMID:Production and characterization of monoclonal antibody to gentamicin. 648 24

Disulfide bonds are a major force in stabilizing the three-dimensional structure of immunoglobulins. To determine the pattern of interchain disulfide bonding between the four H chains, four L chains and single J chain of rat dimeric IgA (dIgA), we analyzed dIgA from the LO DNP-64 hybridoma by diagonal SDS-PAGE. Bands corresponding to one, two, three and four H chains, one and two L chains and the free J chain were observed under non-reducing conditions, suggesting that the interchain disulfide bonds in rat dIgA are unstable under denaturing conditions. Similar patterns of disulfide bonding were observed in three other hybridoma or myeloma dIgAs from LOU/CN rats. In contrast, when dIgA pretreated with iodoacetamide (IA) was analyzed by the same technique, only bands corresponding to four H chains, one and two L chains and the free J chain were observed, suggesting that blocking free sulfhydryl groups stabilizes the inter-H chain disulfide bonds. Reaction of dimeric LO DNP-64 dIgA with 5,5'-dithiobis-(2-nitrobenzoic acid) or with 14C-IA demonstrated that this dIgA contains an average of 4 moles of free sulfhydryl groups per mole of protein under non-denaturing conditions and 9 moles of free sulfhydryl groups under denaturing conditions. Taken together, the results suggest that interchain disulfide bonds in rat dIgA are unstable, presumably due to the influence of nearby free sulfhydryl groups, and that non-covalent forces are critical for stabilizing the dIgA complex. The results also indicate that J chain is entirely non-covalently associated with the H chains, an apparently unique feature of rat dIgA. A model for interchain disulfide bonding in rat dIgA is proposed.
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PMID:Unstable inter-H chain disulfide bonding and non-covalently associated J chain in rat dimeric IgA. 1269 23


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