Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca.

• DOI: 10.1073/pnas.90.3.928
• Publication Date: 2006-05-31T12:39:30Z
• Authors: Y Usami; Y Fujimura; M Suzuki; Y Ozeki; K Nishio; H Fukui; K Titani
• Keywords: Cyanogen bromide; Protein primary structure; Glycoprotein Ib

The complete amino acid sequence and location of the disulfide bonds two-chain botrocetin, which promotes platelet agglutination in presence von Willebrand factor, from venom snake Bothrops jararaca are presented. Sequences alpha beta subunits were determined by analysis peptides generated digestion S-pyridylethylated protein with Achromobacter protease I or alpha-chymotrypsin chemical cleavage cyanogen bromide 2-(2'-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine. Two-chain botrocetin is a heterodimer composed subunit (consisting 133 residues) 125 held together bond. Seven link half-cystine residues 2 to 13, 30 128, 103 120 subunit; 121, 98 113 80 75 subunit. In terms bond location, homologous echinoidin (a sea urchin lectin) other C-type (Ca(2+)-dependent) lectins.