Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom - Archive ouverte HAL Access content directly
Journal Articles Biochemical and Biophysical Research Communications Year : 2000

Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom

(1) , (1) , (1) , (1) , (1) , (1)
1

Abstract

We have investigated the effect of Vipera lebetina venom on capillary permeability and isolated an increasing capillary permeability protein (ICPP) which is devoid of arginine ester hydrolase and phospholipase A2 activities. This protein was purified with a yield of about 0.2% by fast protein liquid chromatography (FPLC) using successively Superose 12, Mono Q, and Mono S columns and by high-pressure liquid chromatography (HPLC) on a C8 reverse-phase column. The purified protein migrated on SDS-PAGE as a band of about 27 kDa under nonreducing conditions and as a band of about 16 kDa under reducing conditions. Chromatography on a C8 column of reduced and alkylated protein yielded a single peak suggesting that this protein is homodimeric. This protein was refractory to Edman degradation chemistry. We used successfully a chemical unblocking involving the incubation of the protein with HCl in anhydrous methanol. The N-terminal amino acid sequence clearly shows considerable similarity to that of vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF).

Dates and versions

pasteur-01984506 , version 1 (17-01-2019)

Identifiers

Cite

Ammar Gasmi, Ferid Abidi, Najet Srairi, Adel Oijatayer, Habib Karoui, et al.. Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom. Biochemical and Biophysical Research Communications, 2000, 268 (1), pp.69-72. ⟨10.1006/bbrc.2000.2078⟩. ⟨pasteur-01984506⟩

Collections

RIIP RIIP_TUNIS
16 View
0 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More