The dependence of somatotropin-binding activity of theca and granulosa tissues of hen preovulatory follicles on pH of incubation buffer was studied. A rise of [125I] somatotropin specific binding to theca tissue with decrease of pH from 6.3 to 5.0 was found to be due predominantly to an increase of the number of somatotropin-binding sites rather than to their affinity. At the same time, the character of change of the level of the hormone specific binding to granulosa cells (at pH 6.0) and to theca crude membrane fraction (at pH 6.7) in the process of development of preovulatory follicles was similar with that revealed at determination of concentration of somatotropin receptors in these tissues at pH 5.0. The obtained data indicate that the majority of somatotropic receptors in hen follicular tissues is latent, at least for in vitro binding, and can be detected at low pH. Nonetheless, the relative changes of somatotropin-binding activity of granulosa and theca tissues in dynamics of folliculogenesis do not depend on pH of incubation medium.

Specific binding of bovine prolactin and somatotropin by granulosa cells from the antral follicles of various diameters was studied in cows at different reproductive states, prepubertal, pubertal, and early gestation. The ability of granulosa cells to bind prolactin did not depend on the reproductive state of an animal. At the same time, the dynamics of somatotropin specific binding by granulosa cells during maturation of the antral follicles differed at dissimilar reproductive states of the cows. When the diameter of follicles increased from 3–5 to 6–10 mm, specific binding of 125 I-somatotropin decreased in pubertal animals, but remained unchanged in the prepubertal and pregnant animals. The results of Scatchard analysis of the binding data indicate that sexual maturation of cows did not affect the binding of prolactin and somatotropin by granulosa cells from follicles of 1–2 mm in diameter. The data obtained suggest that the decreased sensitivity of granulosa cells to somatotropin at the terminal stages of maturation of the antral follicles is essential for their development and acquisition of the ability for ovulation.

A comparative study of effects of Mg2+ ions on specific and competitive binding of the bovine somatotropic hormone (STH) and bovine prolactin (PL) with cells of cow granulosum is carried out. It is found that Mg2+ increases the level of specific binding of 125I-PL with the cells at concentrations from 1 to 70 mM and decreases the level of specific binding of 125I-STH at a concentration of 70 mM. Analysis of the data by Scatchard's method has shown that the decrease of the level of specific binding of 125I-PL in the absence of MgCl2 and 125I-STH at a MgCl2 concentration of 70 mM is caused mainly by a decrease of the number of active binding sites on the cells. Oppositely directed effects of the studied divalent cations on the capability of unlabelled STH (25 µg/ml) and PL (25 µg/ml) for cross-suppression of specific binding of 125I-PL and 125I-STH, respectively, with the granulosum cells have been revealed. At the same time, with increase of Mg2+ ion concentration, the degree of replacement of 125I-STH and 125I-PL with unlabelled STH and PL, respectively, did not change. The obtained results are considered in connection with electrostatic model of participation of the divalent cations in interaction of PL and STH with receptors on cells.

Specific binding of bovine somatotropin (BST) and bovine prolactin (BPRL) to cow granulosa cells from antrumcontaining follicles of different diameter was studied. Scatchard analysis of the data revealed a single type of low affinity BST-binding sites on the granulosa cells with dissociation constants similar to those for the BPRL-binding sites. The number of BST-binding sites on the cells decreased with increasing follicle diameter from 3-5 to 6-10 mm. However, the binding capacity to BPRL decreased only in the case of cells from follicles 11-20 mm in diameter. The findings are discussed in relation to the “homologous binding” phenomenon.