Biochemical and Biophysical Research Communications
Volume 149, Issue 2, 16 December 1987, Pages 744-749
The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin
References (19)
- et al.
Bailliere's Clin. Endocrinol. and Metab
(1987) - et al.
Biochem. Biophys. Res. Commun
(1987) - et al.
Cell
(1986) - et al.
Mol. Cell Endocrinol
(1986) - et al.
Methods. Enzymol
(1983) - et al.
J. Anal. Biochem
(1977) - et al.
Mol. Cell. Endocrinol
(1986) - et al.
Nature
(1986) - et al.
Nature
(1986)
There are more references available in the full text version of this article.
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