Studies on tilapia hepatic growth hormone receptor.
Tilapia liver membranes were solubilized with 1% Triton X-100. The presence of growth hormone (GH) receptors was demonstrated by specific binding of radioiodinated tilapia GH (125I-tGH). The solubilized receptor possessed a molecular weight of around 400,000. It was adsorbed on Con A-Sepharose and DEAE BioGel A indicating that it contains carbohydrates and is acidic in character. Its protein nature was revealed by destruction of GH-binding activity by proteases. The involvement of essential sulfhydryl group was suggested by inhibition of 125I-tGH binding to the solubilized receptor by p-chloromercuribenzene sulfonate which could be reversed by dithioerythritol treatment.
Ng
T B
TB
Department of Biochemistry, Chinese University of Hong Kong, Shatin, N. T.
Leung
T C
TC
Woo
N Y
NY
D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D013006:Growth Hormone / Q000378:metabolism; D008099:Liver / Q000737:chemistry* / Q000378:metabolism; D010473:Perciformes / Q000378:metabolism*; D011986:Receptors, Somatotropin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012995:Solubility
D011986:Receptors, Somatotropin; D002731:4-Chloromercuribenzenesulfonate; D013006:Growth Hormone