Abstract:
:The rainbow trout (Oncorhynchus mykiss) ovarian gonadotropin (GTH II) receptor was solubilized by extraction with the nonionic detergent 1% Triton X-100 in the presence of 20% glycerol. The hormone-binding characteristics of the soluble receptors were similar to those of membrane-bound receptors: the Scatchard plot of the equilibrium binding data produced a straight line, suggesting that the solubilized GTH II receptors, like membrane-bound receptors, contained a single class of high affinity 125I-sGTH II binding sites with an association constant of 2-5 x 10(10) M-1 (Ka = 1.4-2 x 10(10) M-1 for membrane-bound receptor). The maximal binding capacity was very low and varied from 7 to 17 fmol/mg proteins (about 5 fmol/mg ovarian membrane protein). The soluble receptor was purified by a simple and rapid immunoaffinity chromatography. The sGTH II-solubilized receptor complex was adsorbed to anti-sGTH II beta-subunit gammaglobulins covalently linked to Sepharose 4B and then eluted with an acidic buffer. About 50% of the binding activity present in the Triton X-100 extract was recovered in the pH 4 eluate. The other binding sites were eluted as a hormone-receptor complex and/or a damaged form. The free purified receptor presented a Ka of 1.3 x 10(10) M-1 in agreement with those found in membrane preparation and solubilized extract.
journal_name
Gen Comp Endocrinoljournal_title
General and comparative endocrinologyauthors
Quesnel H,Breton Bdoi
10.1006/gcen.1993.1127subject
Has Abstractpub_date
1993-09-01 00:00:00pages
272-80issue
3eissn
0016-6480issn
1095-6840pii
S0016-6480(83)71127-5journal_volume
91pub_type
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