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A study using an iodinated [D-Ser(tBu)6,Pro9-NHEt]LH-RH (Buserelin), demonstrated the presence of a single class of high-affinity (KD = 2.90 nM), high-capacity LH-RH binding sites in pituitaries obtained from sexually mature male and female winter flounder. Displacement curves for unlabeled Buserelin and other preparations of mammalian and fish LH-RH, but a lack of competition for structurally unrelated peptide hormones, indicated the hormone specific nature of the fish pituitary LH-RH receptor preparation. Compared with native mammalian LH-RH and salmon LH-RH, Buserelin and an analog of salmon LH-RH, [D-Arg6,Trp7,Leu8,Pro9-NHEt]LH-RH, had significantly higher binding affinities for the flounder pituitary receptor correlating with results of previous studies demonstrating the superagonist biological activity of LH-RH analogs in trout and goldfish.
L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
February 1976,
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L W Crim, and
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L W Crim, and
R St Arnaud, and
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L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
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L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
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L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
May 1977,
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L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
January 1993,
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L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
May 1976,
General and comparative endocrinology,
L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
January 2014,
PloS one,
L W Crim, and
R St Arnaud, and
M Lavoie, and
F Labrie
September 2003,
European journal of biochemistry,
