Stabilization of basic fibroblast growth factor with dextran sulfate.
Dextran sulfate protected bFGF from heat and acid inactivation and from proteolytic degradation. The protective effect was stronger than that of heparin which is known as a stabilizer of bFGF. Dextran sulfate and bFGF formed a high molecular weight complex via ionic interaction when mixed together in aqueous solution. The complex was dissociated when the ionic strength was increased and the protective effect was completely abolished. Successive digestion of bFGF with Staphylococcus aureus V8 protease and pepsin followed by affinity chromatography on an immobilized dextran sulfate column and reversed-phase high performance liquid chromatography yielded three positively charged fragment peptides, Tyr24-Phe30, Tyr106-Trp114 and Tyr124-Leu138. These results suggest that dextran sulfate stabilizes bFGF by binding close to the putative heparin binding sites of the bFGF molecule.
Kajio
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T
Biotechnology Research Laboratories, Takeda Chemical Industries Ltd., Osaka, Japan.
Kawahara
K
K
Kato
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D016264:Dextran Sulfate / Q000494:pharmacology*; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D016222:Fibroblast Growth Factor 2; D016264:Dextran Sulfate; D002918:Chymotrypsin; D014357:Trypsin; D010434:Pepsin A