1971
DOI: 10.1073/pnas.68.1.63
|View full text |Cite
|
Sign up to set email alerts
|

Synthesis of a Biologically Active N-Terminal Tetratriacontapeptide of Parathyroid Hormone

Abstract: Determination of the amino acid sequence of bovine parathyroid hormone has led to the synthesis of a tetratriacontapeptide corresponding to the aminoterminal 1-34 residues of the native molecule. The specific biological effects of this synthetic peptide on bone and kidney are qualitatively identical to those of the native hormone in classical bioassays in vivo and in several systems in vitro. Potency of the synthetic peptide equals or exceeds that of a biologically active fragment of comparable size isolated f… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

2
87
0

Year Published

1971
1971
2006
2006

Publication Types

Select...
9
1

Relationship

0
10

Authors

Journals

citations
Cited by 200 publications
(89 citation statements)
references
References 14 publications
2
87
0
Order By: Relevance
“…At 0.08 Amol/min isoproterenol was inactive, but at 0.8 /Amol/ min the iPTH levels increased significantly (P < 0.01) ( (17) suggests that the secretion of PTH is increased. However, because the measurements have not been performed in the venous effluent of the parathyroid glands but in peripheral plasma samples, a metabolic alteration of the circulating iPTH peptides cannot be ruled out.…”
Section: Resultsmentioning
confidence: 94%
“…At 0.08 Amol/min isoproterenol was inactive, but at 0.8 /Amol/ min the iPTH levels increased significantly (P < 0.01) ( (17) suggests that the secretion of PTH is increased. However, because the measurements have not been performed in the venous effluent of the parathyroid glands but in peripheral plasma samples, a metabolic alteration of the circulating iPTH peptides cannot be ruled out.…”
Section: Resultsmentioning
confidence: 94%
“…Most of the biological activity of PTH resides in the 1-34 region so that, on a molar basis, PTH(I-34) normally has a potency equal to that of the whole PTH molecule (Potts, Tregear, Keutmann, Niall, Saner, Deftos, Dawson, Hogan and Aurbach, 1971). Similarly, in both the in vivo and in vitro experiments here, the increase in net calcium absorption rate from the rumen associated with the administration of PTH(1-34) was comparable with that found using an equimolar amount of PTHrP(1-34).…”
Section: Discussionmentioning
confidence: 99%
“…Bovine hormonal fragments 1-34, 14-34, 19-34, and 1-13 were synthesized by a modification of the solid phase methods previously described (9). Fragments 1-34, 14-34, and 19-34 were prepared by removing quantities of peptide-resin at the appropriate steps in a single synthesis beginning with resin-esterified phenylalanine.…”
Section: Methodsmentioning
confidence: 99%