title: Isolation and amino acid sequence of the alpha-subunit of follicle-stimulating hormone from equine pituitary glands.
abstract: Six hundred milligrams of follicle-stimulating hormone (FSH), containing 110 NIH-FSH-S1 units/mg, was isolated from 9 kg of equine pituitary glands. The equine FSH was dissociated into alpha- and beta-subunits. A tentative amino acid sequence of the alpha-subunit was determined. The alpha-subunit contained 82 amino acids. The equine FSH-alpha is shorter by 10 to 14 amino acids at the NH2 terminus and has several substitutions at several positions as compared with human FSH-alpha and bovine thyroid-stimulating hormone-alpha. At the intraspecies level, the alpha-subunits of human FSH, human luteinizing hormone, and human chorionic gonadotropin are similar, whereas at the interspecies level there are differences among the alpha-subunits of FSH, luteinizing hormone, and thyroid-stimulating hormone.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005640:Follicle Stimulating Hormone / Q000302:isolation & purification; D006736:Horses; D006801:Humans; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D010902:Pituitary Gland; D013045:Species Specificity
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D005640:Follicle Stimulating Hormone