RESUMO
We describe the production of a mouse monoclonal antibody (H2E1) against human myeloperoxidase antigen. After production and characterisation, this antibody was compared with commercially available monoclonal antibodies, cytochemical myeloperoxidase and previously produced polyclonal antibody. Reaction with various cell lines proved that this monoclonal antibody was specific for myeloid lineage. This monoclonal showed positivity in 81.8 per cent of acute myeloid leukaemias whereas the polyclonal antibody was 100 per cent positive. We found that the polyclonal antibody was more sensitive as compared to the monoclonal. This is probably due to the lack of recognition of individual epitopes on the antigen. We recommend the use of antibodies which have different epitope recognition as most specific for myeloperoxidase.
Assuntos
Animais , Anticorpos Monoclonais/biossíntese , Estudos de Avaliação como Assunto , Humanos , Imuno-Histoquímica , Imunofenotipagem , Leucemia Mieloide/imunologia , Camundongos , Peroxidase/imunologia , Células Tumorais CultivadasRESUMO
To evaluate the binding of human TSH (h-TSH) to various human thyroid tumours using radio receptor assay technique, 26 thyroid tumour specimens were examined. Five specimens did not show displacement by stable h-TSH. A wide variation was observed in B0, non specific binding, affinity and capacity of TSH in all the tumours examined. The Scatchard analysis of the binding of h-TSH to thyroid membranes suggested the presence of the receptors in 57.7 per cent (15 of 26, Ka much greater than 10(9)) and more than one component in 46 per cent (12 of 26) of the tumours studied. There was no consistent pattern of the binding of TSH for thyroid tissue with respect to its pathology. However, with 35 pairs of observations log affinity appeared to be linearly related to log capacity with a slope -0.95, intercept 9.96 and r value -0.93.