Growth Hormone Receptor (GHR) is a kind of transmembraneghicoprotein which consist of a single polypeptide chain. Its physical and biochemical character is typical and determined by its structure.In this paper, purification of growth hormone receptor from ovine liver and identification of its biochemical character have been done.Firstly, by homogenizing, triturating, high-speed centrifuging, hypervelocity centrifuging and sucrose density grade centrifuging cell membrane of ovine liver was separated and its electron microscope slice wasprotein was disL~olved with TritonX-100,amL-thebinding activity between cell membrane or membrane protein and '~I-hGH using RRA(Radio Receptor Assay)was measured, perfect saturated curve wasgained. Thirdly, specific binding of GILR protein was measured ,by SDSPAGE, its molecular weight is about 1 19KD.Furthermore , the influence of temperature and time to binding activity between receptor protein and '~I-hGH was researched. The result indicated the binding activity is the highest in the conditio. of room temperature for 2 hour or 4t for 24 hour.
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