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We have used single- or double-point D-amino acid substitutions to study the structure-function relationships involving residues 32 to 46 of the glycoprotein hormone common alpha-subunit (GPHa) and the testicular follicle-stimulating hormone (FSH) and luteinizing hormone (LH/hCG) receptors. D-Amino acid substitution analogs of GPHa(32-46) were synthesized(More)
Involvement of the third cytoplasmic (3i) loop (residues 533 to 555) of the rat testicular FSH receptor in the mechanism of FSH signal transduction was examined using light membranes prepared from immature rat testes, monolayer cultures of rat Sertoli cells, and a synthetic peptide strategy. This region of the FSH receptor is structurally related to G(More)
This study proposes a rear-surface ablation enhancement approach to fabricate high-aspect-ratio microchannels by temporally shaping femtosecond laser pulse trains. In the case study of K9 glass, enhancements of up to a 56 times higher material removal rate and a three times greater maximum drilling depth are obtained by the proposed method, as compared with(More)
A synthetic peptide strategy was used to study structure-function relationships between residues 32 to 46 of the glycoprotein hormone alpha subunit (GPH alpha) and the testicular follicle-stimulating hormone (FSH) and luteinizing hormone (LH/hCG) receptors. A peptide amide corresponding to this region [GPH-alpha-(32-46)] inhibited both 125I-hFSH and(More)
We previously reported purification of a protein (approximately equal to 57 kDa) from human follicular fluid having FSH binding inhibitory (FSH-BI) activity. Purified hFSH-BI was cleaved with cyanogen bromide and trypsin. The resulting peptide fragments were separated by HPLC and sequence information for individual fragments was obtained. A ten amino acid(More)
We previously reported that residues 9-30 of the extracellular N-terminus domain of the rat FSH receptor, which has no homologous sequence in receptors for related pituitary glycoprotein hormones, represented a specific FSH binding domain. Further examination of its deduced primary structure identified another region, residues 300-315, which was also unique(More)
We examined the involvement of the carboxyl terminal cytoplasmic domain (residues 645-653) of the rat testicular FSH receptor in FSH signal transduction utilizing light membranes prepared from immature rat testes, intact cultured rat Sertoli cells, and a synthetic peptide approach. This region of the FSH receptor was selected because of its structural(More)
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