Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from Phoneutria nigriventer (armed spider) venom.

Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from Phoneutria nigriventer (armed spider) venom. Toxicon 31, 377-384, 1993. Crude Phoneutria nigriventer venom was fractionated by Sephadex, ion-exchange and reverse-phase high performance liquid chromatography. One protein (PNV1) with spasmogenic activity in rabbit vascular smooth muscle was isolated and biochemically characterized. PNV1 has 125 amino acid residues and a calculated mol. wt of 13,899. Special features of the amino acid composition of PNV1 are the presence of two disulfide bridges and the high percentage (27%) of Asx and Glx. The N-terminal amino acid sequence indicates that PNV1 is different from other polypeptides isolated from Phoneutria nigriventer venom.