[Purification of follicle-stimulating hormone from human pituitary glands].
نویسنده
چکیده
A highly purified follicle-stimulating hormone from human pituitary glands has been prepared by ammonium sulfate and ethanol fractionation, gel filtration on Sephadex G-100, ion exchange chromatography on carboxymethyl cellulose, zone electrophoresis on cellulose columns, and preparative continuous flow polyacrylamide gel electrophoresis. The final product has shown lO,OOO-fold purification over the crude pituitary acetone powder. The follicle-stimulating hormone has sedimented as a single boundary in the ultracentrifuge with an ~~0,~ value of 2.04, has shown a single zone in polyacrylamide disc electrophoreses at pH 8.6 and pH 4.3, and has shown a single precipitin line in immunoelectrophoresis in agar against anti-follicle-stimulating hormone sera produced in rabbits. The purified follicle-stimulating hormone contained 185 NIH-FSH-S3 and less than 0.02 NIH-LH-S4 (luteinizing hormone) units per mg, and was free of pituitary, thyrotropic, growth, prolactic, and adrenocorticotropic hormones.
منابع مشابه
Purification of Follicle-stimulating Hormone from Human Pituitary Glands*
A highly purified follicle-stimulating hormone from human pituitary glands has been prepared by ammonium sulfate and ethanol fractionation, gel filtration on Sephadex G-100, ion exchange chromatography on carboxymethyl cellulose, zone electrophoresis on cellulose columns, and preparative continuous flow polyacrylamide gel electrophoresis. The final product has shown lO,OOO-fold purification ove...
متن کاملIsolation and physicochemical characterization of luteinizing hormone from human pituitary glands.
Luteinizing hormone containing 8.9 NIH-LH-Sl units per mg was isolated from human pituitary glands by isoelectric focusing in a sucrose gradient containing carrier ampholytes. Approximately 88% of the starting units was recovered, suggesting no apparent loss or inactivation of the hormone activity during isolation procedures. The luteinizing hormone showed a single protein band in acrylamide di...
متن کاملIN THIS ISSUE Review: •Human Pituitary Hormones Tips and Techniques: •A Guide to Hormone Reference Preparations
As the primary regulator of the endocrine system, the pituitary gland is the most important of the endocrine glands. The major glands of the endocrine system include the pituitary, thyroid, and parathyroid glands, and the pancreas, adrenal cortex, ovaries, and testes. The pituitary regulates the actions of most of these glands and many other body functions. It, in turn, is regulated by the hypo...
متن کاملAmino acid sequence of the beta subunit of follicle-stimulating hormone from human pituitary glands.
The beta subunit of follicle-stimulating hormone (FSH-beta) from human pituitary glands was reduced and S-aminoethylated prior to thermolytic, tryptic, and chymotryptic digestions. Each digest was gel-filtered on Sephadex G-50 to seperate the glycopeptides. The glycopeptides and the peptides were isolated by high voltage paper electrophoresis at pH 6, 3.5, and 2.0. The purity of the isolated pe...
متن کاملIsolation and amino acid sequence of the alpha-subunit of follicle-stimulating hormone from equine pituitary glands.
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 termin...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine
دوره 98 4 شماره
صفحات -
تاریخ انتشار 1958