RESUMEN
The article presents the experimental study results of a comparative assessment of the allergenic activity of three newly developed veterinary preparations (both their major components and complete combined forms)--rivicycline, sulphapen and geovet . No increase in sensibilization was traced, and some indicators showed a weakened sensitizing ++ action of the combined preparations in comparison with the respective doses of the constituent allergic components. The allergy inducing components were determined. The authors recommended hygienic norm of the combined veterinary preparations, as mixtures with permanent composition, by their major allergic components. The proposed technique of a comparative express-test of allergic mixtures and their components may be recommended as another approach to express hygienic norming of the allergens.
Asunto(s)
Metenamina/efectos adversos , Oxitetraciclina/efectos adversos , Penicilina V/efectos adversos , Rifampin/efectos adversos , Sulfametoxipiridazina/efectos adversos , Tetraciclina/efectos adversos , Animales , Quimioterapia Combinada/administración & dosificación , Quimioterapia Combinada/efectos adversos , Cobayas , Metenamina/administración & dosificación , Oxitetraciclina/administración & dosificación , Penicilina V/administración & dosificación , Rifampin/administración & dosificación , Sulfametoxipiridazina/administración & dosificación , Tetraciclina/administración & dosificaciónRESUMEN
The thermal inactivation kinetics of glucose-6-phosphate dehydrogenase during ageing of human diploid cells were studied. It was shown that semi-logarithmic anamorphisms of the thermal inactivation kinetic curves may be presented as a total of two rectilinear sites corresponding to the thermolabile and thermostable fractions of the enzyme. In ageing cells the enzyme stability is decreased as compared to the young ones due to the increase in the amount of the thermolabile fraction. It was also found that despite a certain variability in the process of the cell growth at the 22nd passage the thermal stability of glucose-6-phosphate dehydrogenase is decreased, while the enzyme thermal stability in the cells at the 52nd passage is monotonously increased. Purification of the enzyme from ageing and young human diploid cells results in an increase of the enzyme stability. However, when the enzyme was isolated from young cells, it possessed a higher thermal stability.
Asunto(s)
Glucosafosfato Deshidrogenasa/metabolismo , Línea Celular , Diploidia , Humanos , Cinética , Factores de TiempoRESUMEN
A new procedure for purification of glucose-6-phosphate dehydrogenase resulting in an electrophoretically homogenous preparation made up of 5.10(8) cells (390 mg of protein) is proposed. The enzyme yield is more than 20%. The molecular weights of a subunit and a native enzyme are 55000 and 220000, respectively. The isoelectric point for the protein lies at 4,8. The kinetics of the enzyme thermal inactivation obey the first order equation with the inactivation rate constant of 6.10(-3) min-1.
Asunto(s)
Glucosafosfato Deshidrogenasa/aislamiento & purificación , Células Cultivadas , Glucosafosfato Deshidrogenasa/metabolismo , Humanos , Cinética , Sustancias Macromoleculares , Peso MolecularRESUMEN
Two strains of diploid cells were prepared from the lung (BEL-2) and skin-muscle (SMBE-3) tissues of a bovine embryo. According to the results of morphological and karyological studies, these cultures consisted of fibroblast-like cells retaining diploid chromosome number (60) in the process of long-term cultivation. These cell populations have a limited life span (75-80 passages) and 3 growth phases. The species appurtenance of BEL-2 and SMBE-3 cells was confirmed. The cells were not contaminated with mycoplasma or extraneous viruses, had no tumorigenic activity. The BEL-2 cell culture is most susceptible to measles virus, SMBE-3 culture to vaccinia virus.