A Bovine Hypothalamic Peptide Possessing Immunoreactive Growth Hormone-Releasing Activity*
| Autor: | R. M. G. Nair, M. Barnes, J. Antalis, D. L. Wilbur, C. Devillier |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
medicine.medical_specialty
Somatotropic cell Hypothalamus Peptide hormone Growth Hormone-Releasing Hormone Chromatography Affinity Endocrinology Column chromatography Affinity chromatography Anterior pituitary Pituitary Gland Anterior Internal medicine medicine Animals Immunoassay Chromatography Chemistry Adrenalectomy Biological activity Luteinizing Hormone Rats medicine.anatomical_structure Somatostatin Biochemistry Sephadex Biological Assay Cattle Spectrophotometry Ultraviolet Follicle Stimulating Hormone Peptides |
| Zdroj: | Endocrinology. 103:112-120 |
| ISSN: | 1945-7170 0013-7227 |
| DOI: | 10.1210/endo-103-1-112 |
| Popis: | A systematic search for a GH-releasing factor (GHRF) was carried out using bovine hypothalamic extracts. Purification by Sephadex G-25 column chromatography yielded 17 crude polypeptide peaks distributed over 720 fractions. These were separately pooled, lyophilized, and tested in vivo in rats for GH-releasing activity. Only two peaks (X and X1) were active (50 μg) in releasing immunoreactive GH from the rat anterior pituitary. Small portions of this crude material were purified by affinity chromatography on a column packed with agarose-bound somatostatin antibody, and the resultant somatostatin-free product was active (100 ng) in rats in vivo, showing a 9-fold increase of immunoreactive GH. Thin layer chromatographic mobility of the GH-releasing peptide was different from that of a previously reported GHRF and other known peptide hormones. Lack of inactivation of the GHRF by aminopeptidase, the negative results of Edman-dansyl degradation, and the destruction of the biological activity by pyrrolidone carb... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|