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אסיף מאגר המחקר החקלאי
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Isolation and purification of avian parathyroid hormone using high performance liquid chromatography, and some of its properties
Year:
1984
Authors :
Bär, Arie
;
.
Hurvitz, Shmuel (Animal science)
;
.
Pines, Mark
;
.
Volume :
53
Co-Authors:
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Bar, A., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Facilitators :
From page:
224
To page:
231
(
Total pages:
8
)
Abstract:
A peptide has been extracted in acetic acid from the parathyroid glands of chicks (Gallus domesticus) raised on a vitamin D-deficient diet. The peptide was purified by gel filtration and high-performance liquid chromatography (HPLC). Its degree of purity was ascertained also by SDS-polyacrylamide gel electrophoresis. The avian hormone had the same SDS electrophoretic mobility as bovine parathyroid hormone (bPTH) and therefore a similar molecular weight. The avian peptide was lower than bPTH in basic amino acids and considerably higher in glycine. Evidence for the identity of the peptide as avian parathyroid hormone relies on its source, the similarity of its molecular weight to that of bPTH, and its high potency in stimulating cyclic AMP production in kidney cells in vitro and in vivo. © 1984.
Note:
Related Files :
Animal
animal cell
cattle
Chickens
Chromatography, High Pressure Liquid
Cyclic AMP
Male
Show More
Related Content
More details
DOI :
10.1016/0016-6480(84)90246-6
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21965
Last updated date:
21/08/2022 07:45
Creation date:
16/04/2018 23:48
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Scientific Publication
Isolation and purification of avian parathyroid hormone using high performance liquid chromatography, and some of its properties
53
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Bar, A., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Isolation and purification of avian parathyroid hormone using high performance liquid chromatography, and some of its properties
A peptide has been extracted in acetic acid from the parathyroid glands of chicks (Gallus domesticus) raised on a vitamin D-deficient diet. The peptide was purified by gel filtration and high-performance liquid chromatography (HPLC). Its degree of purity was ascertained also by SDS-polyacrylamide gel electrophoresis. The avian hormone had the same SDS electrophoretic mobility as bovine parathyroid hormone (bPTH) and therefore a similar molecular weight. The avian peptide was lower than bPTH in basic amino acids and considerably higher in glycine. Evidence for the identity of the peptide as avian parathyroid hormone relies on its source, the similarity of its molecular weight to that of bPTH, and its high potency in stimulating cyclic AMP production in kidney cells in vitro and in vivo. © 1984.
Scientific Publication
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