| 摘要 |
<p>A growth factor is purified by affinity chromatography on a resin I based on polysaccharides on which is fixed heparine in order to obtain a fraction F comprised of traces of the factor aFGF and of a new proteinic fraction by elution with a neutral pH buffer having an ionic force equivalent to that of a NaCl solution close to 1M, and the above mentioned fraction F is purified by affinity chromatography on a resin II by elution with a neutral pH buffer of an ionic force equivalent to that of a NaCl solution close to 2M, the resin II being a cross-linked dextrane presenting carboxymethyl, optionally carboxymethylbenzylamide, and carboxymethylbenzylamide sulfonate functions, and of which the biological behaviour is that of heparine. The new proteinic fraction is characterized in that its molecular weight is determined as being 20,000 D in electrophoresis in non-reducing conditions (single band spectrum), and as being 19,000 D in electrophoresis in reducing conditions (dual band spectrum), and in that, by HPLC, it provides a three-peak spectrum.</p> |
