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261.
Luiz Henrique Soares de Andrade Wilson Max Almeida Monteiro de Moraes Eduardo Hiroshi Matsuo Junior Elizabeth de Orleans Carvalho de Moura Hanna Karen Moreira Antunes Jairo Montemor Ednei Luiz Antonio Danilo Sales Bocalini Andrey Jorge Serra Paulo José Ferreira Tucci Patricia Chakur Brum Alessandra Medeiros 《Molecular and cellular biochemistry》2015,402(1-2):193-202
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Patricia Easterbrook Roberts 《Arts Education Policy Review》2013,114(4):153-172
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Terence E. Nicholas Rodger G. Johnson Moira A. Lugg Patricia A. Kim 《Life sciences》1978,22(17):1517-1524
Incubation of fetal lung tissue with 0.2 μM 14C-cortisone revealed a 12-fold increase in the rate of reduction of cortisone to cortisol between day 22 and day 30 of gestation in the rabbit. This increase correlated closely with the increase in the rate of incorporation of 14C-choline into total lung lipids during the same period. In light of these findings it would seem inadequate to attempt to relate the plasma cortisol concentration alone with the rate of lung maturation. In addition, one would need consider both the plasma concentration of cortisone and the activity of 11β-hydroxysteroid dehydrogenase (11β-HSD) in the lung. 相似文献
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Mark E. Costlow Patricia E. Gallagher 《Biochimica et Biophysica Acta (BBA)/General Subjects》1979,587(2):192-201
Concanavalin A, which binds to specific carbohydrate determinants on the cell surface, was used to investigate the binding of prolactin to its receptors in liver membranes from female rats. The binding of 125I-labeled ovine prolactin to receptors was sharply inhibited by concanavalin A. This effect was reversed by the competitive sugar α-methyl-D-mannopyranoside and thus required the presence of specifically bound lectin. Concentrations of concanavalin A of up to 50 μg/ml caused a progressive decrease in the apparent affinity of the prolactin receptor for hormone. When higher concentrations were used, the number of available binding sites decreased. Concanavalin A-resistant receptors, about 30% of the total, had the same dissociation constant (Kd) as the controls. The binding of 125I-labeled concanavalin A in the same membrane preparations showed the presence of two distinct types of concanavalin A binding. At low concentrations, the lectin bound with high affinity (Kd ≈ 6.6 · 10?8 M). At high lectin concentrations, low affinity (Kd ≈ 6.7 · 10?5 M) binding predominated. Since high affinity concanavalin A binding was saturated at 50 μg/ml, this class of binding most likely alters the affinity of the prolactin receptor for hormone; low affinity concanavalin A binding may mask prolactin receptors, making them inaccessible to the hormone.Binding sites for concanavalin A and prolactin appear to be independent but closely related since (i) concanavalin A did not displace bound prolactin from its receptor, and (ii) detergent-solubilized 125I-labeled prolactin-receptor complexes bound to concanavalin A-Sepharose and were eluted by α-methyl-D-mannopyranoside. 相似文献
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