Artículos de revistas
Biochemical Characterization Of A Vascular Smooth Muscle Contracting Polypeptide Purified From Phoneutria Nigriventer (armed Spider) Venom.
Registro en:
Toxicon : Official Journal Of The International Society On Toxinology. v. 31, n. 4, p. 377-84, 1993-Apr.
0041-0101
8503129
Autor
Marangoni, S
Borges, N C
Marangoni, R A
Antunes, E
Vieira, C A
Novello, J C
Domont, G B
Giglio, J R
Oliveira, B
de Nucci, G
Institución
Resumen
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. 31 377-84