Purification of heparin-binding growth factors

Properties of heparin binding to purified plasma membranes from bovine granulosa cells

“…This is consistent with reports that binding of heparin to membrane-associated domains can be disrupted by increased ionic strength (Lobb et al, 1986). Furthermore, the gradual displacement of the radiolabel (as opposed to an all-or-none response) suggested that multiple binding domains with different affinities for heparin might be involved.…”

“…In contrast, the anionic steroid detergent cholic acid may have ionized non-polar amino acids from the hydrophobic region of the proteins, potentially increasing electrostatic interactions between the binding proteins and heparin. The zwitterionic cholic acid derivative CHAPS solubilizes membranes without causing ionization or allowing aggregation which might alter the biological activity of membrane-bound proteins (Hjelmeland, 1980 (Lobb et al, 1986). Reduction of disulphide bonds with 5% 2-mercaptoethanol before electrophoresis had no effect on the apparent molecular weights or ability to bind heparin of such proteins (Winer & Ax, 1989).…”

Biological impact of the fibroblast growth factor family on articular cartilage and intervertebral disc homeostasis

“…Basic FGF, a well-known member of the FGF family, was originally isolated and identified from bovine brain and pituitary based on its stimulatory activity on fibroblast proliferation (Bohlen et al, 1984;Lobb et al, 1986). It has been extensively studied in the literature and is found to be involved in numerous cellular functions in various cell types, including angiogenesis, tumorigenesis, cell proliferation, differentiation, wound healing, limb formation, and tissue remodeling (Bodo et al, 2002;Bobick et al, 2007;Douwes Dekker et al, 2007;Kakudo et al, 2007;Kanayama et al, 2007;Pratsinis and Kletsas, 2007;Schmal et al, 2007;Choi et al, 2008).…”

Purification and Characterization of Novel Heparin-binding Growth Factors in Uterine Secretory Fluids

“…1A). The elution position of this factor (hereafter termed HBGF-0.8) from heparin affinity columns was clearly distinct from PDGF, HB-EGF, PTN, aFGF, bFGF, and amphiregulin (2,8,12,(22)(23)(24). Stability tests performed by exposing HBGF-0.8 to pH 1.5 for 2 min, 56°C for 30 min, or 100°C for 5 min demonstrated that the 3T3 cell mitogenic activity of HBGF-0.8 was highly susceptible to acid or heat inactivation (data not shown).…”