Category Archives: Hormone - Part 4

Hormone-Specific Inhibitory Influence: MATERIALS AND METHODS(4)

The truncated eLHp derivative, deseLHp (hereafter abbreviated eLHpt), was prepared by mild acid hydrolysis of eLHp followed by Sephacryl S-200 chromatography as previously reported . The truncated eCGp derivative, deseCGp (eCGpt), was also prepared by mild acid hydrolysis. Reverse-phase HPLC … Continue reading

Hormone-Specific Inhibitory Influence: MATERIALS AND METHODS(3)

Preparation of Hybrid Hormones Hybrid hormones were prepared on an analytical scale by combining 80-|xg samples of each subunit preparation in 0.5 M Tris-acetate buffer, pH 7.0, for 72 h at 37°C. All possible combinations of native or aAsn56-deglycosylated equine … Continue reading

Hormone-Specific Inhibitory Influence: MATERIALS AND METHODS(2)

The eFSH receptor-binding activity of the eFSHa preparation was 2.8% (relative to eFSH), while that of the eFSHp preparation was 4.3% using l25I-eFSH and a Chinese hamster ovary (CHO) cell line expressing the hFSH receptor (hFSHR). Matrix assisted laser-desorption ionization, … Continue reading

Hormone-Specific Inhibitory Influence: MATERIALS AND METHODS(1)

Hormone Subunit Preparations Purification and characterization of eFSH, eLH, and eCG-M (“medium” molecular weight) were described earlier . Dissociation of the purified hormones into subunits in 6 M guanidine, separation of a and (3 subunits of eLH and eCG-M by … Continue reading

Hormone-Specific Inhibitory Influence of a-Subunit Asn56 Oligosaccharide on In Vitro Subunit Association and Follicle-Stimulating Hormone Receptor Binding of Equine Gonadotropins(3)

It is generally accepted that receptor-binding activity of gonadotropins is determined primarily by their hormone-specific P subunits . The influence of the common a subunit on receptor-binding affinity of gonadotropins has been reported to be insignificant . However, this concept … Continue reading

Hormone-Specific Inhibitory Influence of a-Subunit Asn56 Oligosaccharide on In Vitro Subunit Association and Follicle-Stimulating Hormone Receptor Binding of Equine Gonadotropins(2)

The homologous mammalian residue can be determined by adding 4 to the ha residue number.) Since haAsn52 (homologous to equine a-subunit Asn56) oligosaccharide is located close to the residues involved in subunit interaction, this carbohydrate may affect subunit heterodimerization by … Continue reading

Hormone-Specific Inhibitory Influence of a-Subunit Asn56 Oligosaccharide on In Vitro Subunit Association and Follicle-Stimulating Hormone Receptor Binding of Equine Gonadotropins(1)

Equine (e) FSH, eLH, and eCG are heterodimeric glycoproteins consisting of a common a subunit glycosylated at Asn56 and Asn82 and a hormone-defining, variably glycosylated p subunit. The crystal structure of hCG has revealed the glycoprotein hormones to be members … Continue reading

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