Identification and Partial Purification of a Basic Fibroblast Growth Factor-Like Growth Factor Derived from Bovine Colostrum
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چکیده
منابع مشابه
Purification and partial sequence analysis of insulin-like growth factor-1 from bovine colostrum.
Growth-promoting activity in bovine colostrum has been detected as the capacity to stimulate protein synthesis in L6 myoblasts. By using this assay as a measure of bioactivity, a growth factor has been purified to near homogeneity from centrifuged colostrum by a series of steps including acid extraction, chromatography on sulphopropyl-Sephadex, followed by adsorption to, and elution from, C18 c...
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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...
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The purification of the fibroblast growth factor (FGF) from bovine brain has led to the isolation of two peptides. FGF-1 with 128 amino acids and FGF-2 with 107 amino acids. The biological activity of these two peptides is acid- and heat-labile. As indicated by the amino acid composition of FGF-1 and -2, these two peptides are derived from a common precursor and bear no resemblance to pituitary...
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A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chlo...
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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...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1997
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(97)75961-7