Identification and characterization of growth hormone receptors in snakehead fish (Ophiocephalus argus Cantor) liver
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AbstractThe specific binding of I-125-labeled fish growth hormone (GH) to hepatic membranes prepared from several freshwater fish was assessed. A high level of growth hormone receptor (GHR) was detected on the hepatic membranes of the snakehead fish (Ophiocephalus argus Canter). Scatchard analysis of the binding data showed a single class of high affinity binding site with a binding affinity (K-a) of 1.45 +/- 0.23 x 10(9) M-1 and a binding capacity (B-max) of 198 +/- 57 fmol/mg protein. The binding was specific for fish GH and was saturable. In addition, the specific binding was temperature-and time-dependent, reaching a steady state after 16 hr of incubation at 25 degrees. The molecular weight of GHR as measured by Sephadex G-200 column chromatography and Western blot analysis using a monoclonal antibody (Mab263) against GHR was found to be 200-400 and 90-93 kDa, respectively. Two bands at 65 and 89 kDa were identified in ligand crosslinking studies of membrane receptors. A sensitive teleost GH radioreceptor assay (RRA) was developed, using recombinant fish GH and a membrane preparation from snakehead fish liver, capable of measuring bioactive GH in fish sera or other samples. (C) 1997 Academic Press.
All Author(s) ListSun X, Zhu SQ, Chan SSH, Toresson G, Cheng CHK
Journal nameGeneral and Comparative Endocrinology
Year1997
Month12
Day1
Volume Number108
Issue Number3
PublisherACADEMIC PRESS INC ELSEVIER SCIENCE
Pages374 - 385
ISSN0016-6480
eISSN1095-6840
LanguagesEnglish-United Kingdom
Web of Science Subject CategoriesEndocrinology & Metabolism; ENDOCRINOLOGY & METABOLISM

Last updated on 2020-22-10 at 00:55