Presence of subunit structure in bovine follicle-stimulating hormone.
Highly purified bovine follicle-stimulating hormone (FSH) potency 164 X NIH-FSH-S-1 by bioassay was estimated to be 210 +/- 4.2 X NIH-FSH-S-1 by radioligant-receptor assay using 125I-bovine FSH as tracer but only 120 +/- 1.8 X NIH-FSH-S-1 when 125I-human FSH tracer was used. The presence of subunit structure in bovine FSH was revealed by SDS-polyacrylamide gel electrophoresis. Furthermore, treatment of bovine FSH with 1 M propionic acid resulted in marked changes of mobilities upon polyacrylamide gel electrophoresis and elution profiles after gel filtration on Sephadex G-100 in addition to loss of biological activity by radioligand-receptor assay. After incubation, the propionic acid-treated bovine FSH recovered about 75% of the receptor-binding activity and regenerated protein bands of identical electrophoretic mobilities as the native hormone.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D004305:Dose-Response Relationship, Drug; D004589:Electrophoresis, Disc; D005640:Follicle Stimulating Hormone; D046911:Macromolecular Substances; D011485:Protein Binding; D011869:Radioligand Assay; D013045:Species Specificity
D046911:Macromolecular Substances; D005640:Follicle Stimulating Hormone