Purification and Characterization of Pituitary Bovine Somatotropin
نویسندگان
چکیده
منابع مشابه
Purification and characterization of pituitary bovine somatotropin.
Bovine somatotropin (bST) has been isolated from pituitary glands and compared in a variety of chemical analyses and bioassays with somatotropin derived from recombinant Escherichia coli. Comparison of pituitary extracts and purified bST by Western blot analysis of two-dimensional gels suggested that the immunoreactive somatotropin species present in the extract were also present in the purifie...
متن کاملPurification and characterization of the D2-dopamine receptor from bovine anterior pituitary.
The D2-dopamine receptor from bovine anterior pituitary has been purified approximately 33,000-fold to apparent homogeneity by sequential use of affinity chromatography on immobilized carboxymethyleneoximinospiperone-Sepharose, Datura stramonium lectin-agarose, and hydroxylapatite chromatography. The purification yields a single polypeptide band of Mr approximately 120,000 on sodium dodecyl sul...
متن کاملPurification and partial characterization of an acidic fibroblast growth factor from bovine pituitary.
Isoelectric focusing has allowed us to fractionate pituitary extracts into basic (pI 8-9) and acidic (pI 4-5) fibroblast growth factor. The acidic fibroblast growth factor (a) is stable upon refocusing, (b) migrates as an acidic protein in urea-containing gel electrophoresis; (c) is not cell-specific, being active with fibroblasts, adrenal, and glial cells, and (d) is a heterogeneous protein fr...
متن کاملPurification and characterization of bovine placental lactogen.
Bovine placental lactogen (bPL) was purified 4,200-fold from cotyledon homogenates by 1) salt precipitation and 2) ultrafiltration, followed by 3) gel filtration, 4) anion exchange, 5) hydroxylapatite, 6) chromatofocusing, and 7) final gel filtration chromatography. Purification was monitored by radioreceptor assay (RRA) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. During chro...
متن کاملPurification of a fibroblast growth factor from bovine pituitary.
The purification from bovine pituitary gland of a growth factor responsible for the control of animal cell division in tissue culture is reported. This growth factor is a polypeptide of 13,300 molecular weight and is homogeneous when analyzed by polyacrylamide gel electrophoresis, carboxymethyl-Sephadex gradient elution chromatography, and Sephadex G-50 chromatography. The yield of growth facto...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63761-5