## Abstract 1α‐hydroxycholesterol (**4a**) was synthesized from cholesterol and transformed __via__ its diacetyl derivative **4b** into 1α, 3β‐diacetoxycholesta‐5, 7‐diene (**6b**). Irradiation of the ring‐B‐diene **6b** followed by thermal isomerization and saponification gave 1α‐hydroxycholecalci
Synthese der Sequenz 1-34 von menschlichem Parathormon. Vorläufige Mitteilung
✍ Scribed by R. H. Andreatta; A. Hartmann; A. Jöhl; B. Kamber; R. Maier; B. Riniker; W. Rittel; P. Sieber
- Publisher
- John Wiley and Sons
- Year
- 1973
- Tongue
- German
- Weight
- 232 KB
- Volume
- 56
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
Abstract
Brewer et al. [1] have established sequence I for the first 34 amino acid residues of human parathyroid hormone. It differs in 6 and 5 positions respectively from the corresponding bovine [2] [3] and porcine [4] hormone sequences. The synthesis of the protected tetratriacontapeptide II by the fragment‐coupling approach and its purification by counter‐current distribution are described. Removal of the protecting groups by acidolysis then gave I in high purity.
I displays hypercalcemic activity in the thyroparathyroidectomized rat indicating that the amino terminal part also constitutes the hormonally active region of human parathyroid hormone.
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