Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Geoffrey William Tregear"'
Autor:
D. Scanlon, M. Cronk, Hugh D. Niall, Peter J. Hudson, John D. Haley, John Shine, Geoffrey William Tregear, M. John
Publikováno v:
DNA. 1:155-162
Relaxin is a peptide hormone produced by the corpora lutea of ovaries during pregnancy, softening and lengthening the ligaments of the pelvis and softening the cervix in order to make childbirth easier. In attempts to determine the nucleotide sequenc
Autor:
Peter J. Hudson, Robert J. Crawford, Geoffrey William Tregear, D. Scanlon, John D. Haley, John Shine, Hugh D. Niall
Publikováno v:
Journal of Biological Chemistry. 262:11940-11946
A porcine genomic cosmid library was constructed to study the structure and regulation of the porcine relaxin gene. Two overlapping cosmids containing relaxin-specific sequences were isolated, and a 9-kilobase BamHI fragment containing the porcine re
Publikováno v:
Endocrine Research Communications. 3:407-419
We have studied the effects of guanylylimidodiphosphate (Gpp(NH)p), an analogue of GTP, on the stimulation of renal cortical adenylyl cyclase by bovine parathyroid hormone (bPTH, or bPTH-(1-84)). Incubation of canine renal membranes with bPTH-(3-34),
Autor:
David Goltzman, Henry T. Keutmann, Geoffrey William Tregear, Michael Rosenblatt, John T. Potts
Publikováno v:
Journal of Biological Chemistry. 251:159-164
Several analogues of the biologically active fragment of bovine parathyroid hormone (bPTH), based on the sequence of the NH2-terminal 34 amino acids, were prepared by solid phase synthesis and bioassayed in the in vitro adenylyl cyclase assay to prov
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 42:520-530
A radioimmunoassay for human proparathyroid hormone (hProPTH) has been developed and applied to an evaluation of prohormone content in parathyroid tissues and in plasma. Antisera were produced in rabbits by immunization with a synthetic octadecapepti
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 44:420-423
To gain further insight into the biological significance of parathyroid hormone (PTH) metabolism, native parathyroid hormone and synthetic peptides, similar to PTH metabolites generated in vivo, have been given intravenously to human subjects. The re
Publikováno v:
Endocrinology. 97:1270-1280
The metabolism of natural and synthetic analogues of bovine proparathyroid hormone (Pro-bPTH) and the biological activity of the synthetic fragments were evaluated in an in vitro assay employing renal cortical membranes (adenylyl cyclase bioassay). A
Publikováno v:
Journal of Biological Chemistry. 250:3199-3203
Two synthetic analogues of bovine parathyroid hormone (PTH) with NH2-terminal modifications, PTH-(3-34) and [desamino-Ala-1]PTH-(1-34), were found to lack agonist activity but to demonstrate antagonist properties when tested in the rat renal cortical
Autor:
P. J. Gaillard, M. P. M. Herrmann-Erlee, J. A. Parsons, J. W. Hekkelman, John T. Potts, Geoffrey William Tregear, J. N. M. Heersche
Publikováno v:
Endocrine Research Communications. 3:21-35
The biological activities of bovine parathyroid hormone (BPTH) and fragments comprising portions of its amino-terminal sequence have been compared in three different assay systems using embryonic rat bone in vitro. Whereas the 3-34 fragment was witho
Publikováno v:
Endocrine Research Communications. 1:1-17
A sensitive radioimmunoassay has been developed to bovine proparathyroid hormone which employs an antiserurm produced by immunization of rabbits with a synthetic 18-amino acid peptide fragment of the bovine prohormone. The synthetic prohormone fragme