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.
Department of Biochemistry, University of Campinas (UNICAMP), SP, Brazil.
S
S
Marangoni
N C
NC
Borges
R A
RA
Marangoni
E
E
Antunes
C A
CA
Vieira
J C
JC
Novello
G B
GB
Domont
J R
JR
Giglio
B
B
Oliveira
G
G
de Nucci
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D007202:Indicators and Reagents; D008297:Male; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects*; D010455:Peptides / Q000032:analysis* / Q000302:isolation & purification / Q000494:pharmacology; D011817:Rabbits; D013111:Spider Venoms / Q000737:chemistry* / Q000494:pharmacology
D007202:Indicators and Reagents; D010455:Peptides; D013111:Spider Venoms