Partial Purification and Characterization of Chicken Corticosteroid-Binding Globulin
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چکیده
منابع مشابه
Specific binding of human corticosteroid-binding globulin to cell membranes.
Specific binding sites for corticosteroid-binding globulin were detected on membranes prepared from human prostates. The binding sites are typical of membrane receptors: they are saturable and specific and have high affinity. There was little specific binding at 4 degrees C and 23 degrees C. Maximal specific binding was obtained at 37 degrees C. Scatchard analysis revealed the presence of a sin...
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Corticosteroid-binding globulin was isolated from normal human plasma by successive anion exchange chromatography and gel filtration. Ammonium sulfate fractionation was employed as a preliminary step when large volumes were processed. The purification was about 4000-fold. Homogeneity was shown by free boundary, agar and paper electrophoresis, sedimentation velocity, and diffusion. Immunoelectro...
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A bstract. Platelets have been shown to affect the growth of vascular endothelial cells. This report describes the characterization and partial purification from human platelets of a novel growth factor which can stimulate human endothelial cells to synthesize DNA and grow. Platelets were lysed by sonication and the particulate fraction removed by ultracentrifugation at 100,000 g. The supernata...
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Chicken pepsinogen was extracted from the forestomach of chicken and purified by the consecutive application of acetone precipitation, chromatography on diethylaminoethyl cellulose, and gel filtration on Sephadex G-100. The purified pepsinogen was homogeneous on disc electrophoresis and sedimented as monodisperse material. Chicken pepsin was obtained by the activation of the pure zymogen at pH ...
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ژورنال
عنوان ژورنال: Poultry Science
سال: 1978
ISSN: 0032-5791
DOI: 10.3382/ps.0571733