Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from phoneutria nigriventer (armed Spider) venom
N.C. Borges, E. Antunes, R.A. Marangoni, B. Oliveira, S. Marangoni, G.B. Domont, J.C. Novello, G. De Nucci, C.A. Vieira, J.R. Giglio
ARTIGO
Inglês
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...
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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
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Fechado
Antunes, Edson, 1960-
Autor
Marangoni, Sergio, 1951-
Autor
Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from phoneutria nigriventer (armed Spider) venom
N.C. Borges, E. Antunes, R.A. Marangoni, B. Oliveira, S. Marangoni, G.B. Domont, J.C. Novello, G. De Nucci, C.A. Vieira, J.R. Giglio
Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from phoneutria nigriventer (armed Spider) venom
N.C. Borges, E. Antunes, R.A. Marangoni, B. Oliveira, S. Marangoni, G.B. Domont, J.C. Novello, G. De Nucci, C.A. Vieira, J.R. Giglio
Fontes
Toxicon: an interdisciplinary journal on the toxins derived from animals, plants and microorganisms Vol. 31, no. 4 (Apr., 1993), p. 377-384 |