Purification of acidic fibroblast growth factor from bovine omentum.
Two heparin binding growth factors with different molecular weight, 16.6 kD and 18.6 kD polypeptide, were purified from bovine omentum. The two factors have almost the same affinity to heparin; they were eluted with 1.0 M NaCl from the affinity column. The 16.6 kD polypeptide was found to be acidic fibroblast growth factor by amino acid sequence analysis. The 18.6 kD polypeptide was an N-terminus blocked polypeptide and was suggested to be beta-endothelial cell growth factor. These molecular species may play significant roles in maintaining vascularized structure in omentum and be related to the angiogenic activity of the tissue.
Ohtaki
T
T
Tsukuba Research Laboratories, Takeda Chemical Industries, Ltd., Ibaraki, Japan.
Wakamatsu
K
K
Mori
M
M
Ishibashi
Y
Y
Yasuhara
T
T
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002460:Cell Line; D002850:Chromatography, Gel; D004247:DNA / Q000096:biosynthesis; D005346:Fibroblast Growth Factors / Q000302:isolation & purification* / Q000502:physiology; D005347:Fibroblasts / Q000378:metabolism / Q000502:physiology; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009852:Omentum / Q000032:analysis*
D005346:Fibroblast Growth Factors; D004247:DNA