Characterization and partial purification of parathyroid hormone messenger RNA.
نویسندگان
چکیده
منابع مشابه
Purification and characterization of a receptor for human parathyroid hormone and parathyroid hormone-related peptide.
The human parathyroid hormone (PTH) receptor (hPTH1R), containing a 9-amino acid sequence of rhodopsin at its C terminus, was transiently expressed in COS-7 cells and solubilized with 0.25% n-dodecyl maltoside. Approximately 18 microg of hPTH1R were purified to homogeneity per mg of crude membranes by single-step affinity chromatography using 1D4, a monoclonal antibody to a rhodopsin epitope. T...
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Full-length human parathyroid hormone-related protein (PTHrP-(1-141] as well as a carboxyl-terminal shortened form (PTHrP-(1-108] have been expressed from recombinant DNA-derived clones. These proteins were expressed in Escherichia coli as fusion proteins so that cyanogen bromide cleavage yields the desired product. Both proteins were purified and then characterized by sodium dodecyl sulfate ge...
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An enzyme fraction containing phosphatase activity for phosphorylated eukaryotic peptide initiation factor 2 (eIF-2) has been isolated from rabbit reticulocytes and partially characterized, The enzyme efficiently catalyzes release of phosphate from the small subunit of eIF-2 (eIF-2a) that has been phosphorylated by the hemin-controlled repressor. It is shown to restore activity of this phosphor...
متن کاملCharacterization and Partial Purification
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...
متن کاملPre-proparathyroid hormone: a direct translation product of parathyroid messenger RNA.
An 8-15S RNA fraction from calf parathyroid glands stimulated the incorporation of radioactive lysine and methionine into protein by 15- to 30-fold in a wheat germ extract. The major product, representing 25% of the total protein synthesized, could be bound to an antiserum to parathyroid hormone and binding was inhibited by parathyroid hormone. The chromatographic mobilities of the two tryptic ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34483-6