Isolation and characterization of chum salmon growth hormone
| Autor: | Akikazu Yasuda, Junko Kubota, Tetsuya Hirano, Hiroshi Kawauchi, Kazuo Yamaguchi, Syunsuke Moriyama, Kunikatsu Shirahata |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Biophysics
Growth Biochemistry Structure-Activity Relationship chemistry.chemical_compound Salmon Animals Amino Acid Sequence Amino Acids Sodium dodecyl sulfate Molecular Biology Gel electrophoresis chemistry.chemical_classification Chromatography biology Histocytochemistry Isoelectric focusing biology.organism_classification Molecular biology Prolactin Amino acid Isoelectric point chemistry Sephadex Growth Hormone Pituitary Gland Oncorhynchus |
| Zdroj: | Archives of Biochemistry and Biophysics. 244:542-552 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(86)90622-3 |
| Popis: | Two molecular forms of salmon growth hormone (sGH), sGH I and II, have been isolated from the pituitary glands of the chum salmon (Oncorhynchus keta); a two-step extraction procedure, under alkaline (pH 10) conditions, subsequent to acid-acetone extraction was employed for extraction of the sGHs. They were then purified by isoelectric precipitation at pH 5.6, gel filtration on Sephadex G-100, and high-performance liquid chromatography on ODS. Intraperitoneal injection of sGH I and a combination of sGH I and II at doses of 0.01 μg and 0.1 μg/g body wt at different intervals resulted in a significant increase in body weight and length of juvenile rainbow trout. The GH producing cells in the pituitary of mature chum salmon were identified in the proximal pars distalis immunocytochemically with a specific antiserum; no cross-reactivity was seen in the prolactin cells in the rostral pars distalis. A molecular weight of 22,000 was estimated for both sGHs by gel electrophoresis in sodium dodecyl sulfate. Isoelectric points, by gel electrofocusing, of 5.6 and 6.0 were estimated for sGH I and II, respectively, with differences present in the amino acid composition and the N-terminal residue, suggesting that they may be genetic variants coded on two separate genes. The partial amino acid sequences of sGH I at both terminal regions have been determined. |
| Databáze: | OpenAIRE |
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