1,721,012 research outputs found
Monoclonal antibodies can reveal immunoreactivity differences between pituitary and recombinant bovine growth hormone
No full textMonoclonal antibodies (MAbs) to pituitary bovine growth hormone (bGH) were used to assay the immunoreactivity of a recombinant form of bGH. The recombinant hormone used differed from the pituitary principally in the presence of a short amino acid sequence starting with methionine added to the N-terminal end of the molecule. Monoclonal antibody 1D2 recognized the recombinant hormone with greater affinity than the pituitary hormone, whereas MAb 5G1 bound the recombinant molecule with a lower strength than the pituitary. The other MAbs showed different behavior depending on the type of immunoassay used. Results indicate that the recombinant bGH molecule has been altered in its immunological structure, and suggest a possible interaction of the added N-terminal fragment with the three-dimensional structure of the hormone
Caratterizzazione elettroforetica di un fattore timico ad attività immunomielomodulatrice.
No full textPeptide mass mapping and N-acetyl- and N-glycolyl-neuraminic acid analysis of pituitary purified bovine follicle stimulating hormone
No full textAn enzyme-linked immunosorbent assay for the determination of bovine prolactin in plasma
No full textHighly purified pituitary bovine prolactin (bPRL) has been used in a sensitive non-competitive enzyme-linked immunosorbent assay of prolactin (PRL) concentrations in plasma. In this assay affinity purified polyclonal antibodies were immobilzed to the solid phase in order to capture the antigen, and were also biotinylated as the detector antibody. The method was found to be reproducible (3% variability between calibration curves) and has been optimized for measuring bPRL concentration in plasma samples, giving an intra-assay coefficient of variation of about 5% and an interassay coefficient of variation of about 9%. The sensitivity of the assay was found to be as low as 0.1 ng/ml of bPRL
Detection of growth hormone in porcine ovarian fluids by a species-specific enzyme immunoassay
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Determinazione immunoenzimatica in fase solida dell'ormone della crescita nel plasma di cavallo con un anticorpo monoclonale e rivelazione in fluorescenza
No full textMonoclonal antibodies as a probe for the unfolding of porcine growth hormone
No full textMonoclonal antibodies (mAbs) were generated against pituitary porcine growth hormone (pGH). Ten mAbs were selected for their specificity and affinity for pGH. These mAbs were of the immunoglobulin G (IgG)1 κ subclass, with dissociation constants (Kd) between 7.42 and 0.26 nM, and recognised seven non-overlapping epitopes. We measured whether the mAbs detected alterations of the pGH three-dimensional structure by comparing the antibody reactivity to native pGH and to pGH experimentally unfolded by heating at 50°C, 75°C and 100°C or by reduction and S-carboxymethylation. The antibody-antigen interactions were studied with two enzyme-linked immunosorbent assays (ELISA), based either on a direct binding or inhibition format. The results show that: 1) one mAb, mAb D12, is a conformation-sensitive antibody that recognises an epitope present only in the native pGH. Because the intact three-dimensional structure is essential for the expression of biological activity, mAb D12 could be used to detect altered pGH molecules in biological samples (blood, pituitary extracts or material produced with recombinant technology), and for the one-step purification of biologically active pGH by immunoaffinity chromatography; 2) one mAb, mAb I4, binds to a linear epitope that is not significantly modified in the denatured hormone. This mAb was able to detect the hormone in assays where protein conformation is usually strongly altered, i.e. immunoblotting and immunohistochemistry; 3) the performances of the other eight mAbs differed significantly in the competitive and non-competitive ELISA
Growth hormone detection in the plasma of cows treated with recombinant bovine growth hormone
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