Publications

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the primary structure of coagulation factor ix/factor x-binding protein isolated from the venom of trimeresurus flavoviridis. homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte fc epsilon receptor for immunoglobulin e.an anticoagulant protein, factor ix/factor x-binding protein (ix/x-bp), isolated from the venom of trimeresurus flavoviridis, binds with factor ix and factor x in the presence of ca2+ with a 1 to 1 stoichiometry (atoda, h., and morita, t. (1989) j. biochem. (tokyo) 106, 808-813). analysis of s-pyridylethylated ix/x-bp by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a 16.0-kda band (designated the a chain) and a 15.5-kda band (designated the b chain). these two chains were s ...19911831197
amino acid sequences of the two subunits of a phospholipase a2 inhibitor from the blood plasma of trimeresurus flavoviridis. sequence homologies with pulmonary surfactant apoprotein and animal lectins.phospholipase a2 inhibitor (pli), purified from the blood plasma of the habu snake (trimeresurus flavoviridis), was separated into two distinct subunits, pli-a and pli-b. these subunits were shown to be glycoproteins with molecular weights of around 21,000-22,000. when they were deglycosylated chemically with trifluoromethanesulfonic acid, the molecular weights were found to be 17,000. their amino acid sequences were determined by alignment of peptides obtained by lysyl endopeptidase digestion a ...19911985928
purification and amino acid sequence of basic protein i, a lysine-49-phospholipase a2 with low activity, from the venom of trimeresurus flavoviridis (habu snake).a basic protein (pi 10.2), named basic protein i, was purified to homogeneity from the venom of trimeresurus flavoviridis (habu snake) after four chromatographic steps. the amino acid sequence of this protein was determined by sequencing the s-pyridylethylated derivative of the protein and its peptides produced by chemical (cyanogen bromide and formic acid) and enzymatic (chymotrypsin, achromobacter protease i, and staphylococcus aureus v8 protease) cleavages. the protein consisted of 122 amino ...19902330604
purification and amino acid sequence of basic protein ii, a lysine-49-phospholipase a2 with low activity, from trimeresurus flavoviridis venom.a basic protein (pi 10.3), named basic protein ii, was purified to homogeneity from the venom of trimeresurus flavoviridis (habu snake) after four chromatographic steps. the amino acid sequence of this protein was determined by sequencing the s-pyridylethylated derivative and its peptides produced by chemical (cyanogen bromide) and enzymatic (chymotrypsin, clostripain, and staphylococcus aureus v8 protease) cleavages. the protein consisted of 122 amino acid residues and was found to be identical ...19902341374
primary structure of hemorrhagic protein, hr2a, isolated from the venom of trimeresurus flavoviridis.the complete amino acid sequence and disulfide bridge location of hr2a, one of the hemorrhagic proteins isolated from the snake venom of trimeresurus flavoviridis, have been determined by analysis of peptides derived from digests with cyanogen bromide, lysyl endopeptidase, trypsin, and staphylococcus aureus v8 protease. peptides were purified by gel filtration followed by reversed-phase hplc. hr2a has the amino-terminal sequence of less than glu-gln-arg- and consists of a total of 202 residues w ...19892753880
primary structure of h2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, trimeresurus flavoviridis.the complete amino acid sequence of and the locations of disulfide bridges in h2-proteinase, a major non-hemorrhagic proteinase isolated from the venom of the habu trimeresurus flavoviridis, have been determined and compared with those of hr2a, one of the hemorrhagic metalloproteinases in this venom. the strategy involved consisted of structural analysis of peptides in digests with cyanogen bromide, lysyl endopeptidase, trypsin, staphylococcus aureus v8 protease and thermolysin. peptides were pu ...19892777746
amino acid sequence of a coagulant enzyme, flavoxobin, from trimeresurus flavoviridis venom.the amino acid sequence of a coagulant enzyme, named flavoxobin, isolated from the venom of trimeresurus flavoviridis (the habu snake) was determined by sequencing the s-pyridylethylated derivative of the protein and its peptides generated by chemical (cyanogen bromide and hydroxylamine) and enzymatic (clostripain, staphylococcus aureus v8 protease, achromobacter protease i, and elastase) cleavages. hydrazinolysis was also employed to determine the c-terminal amino acid. the enzyme consisted of ...19883170503
isolation and amino acid sequence of a phospholipase a2 inhibitor from the blood plasma of agkistrodon blomhoffii siniticus.phospholipase a2 inhibitor (pli) was purified from the blood plasma of chinese mamushi, agkistrodon blomhoffii siniticus, by sequential chromatography on sephadex g-200, mono q, and blue-sepharose cl-6b columns. the purified pli was a glycoprotein with an apparent molecular mass of 75 kda and was composed of a single subunit with a mass of about 20 kda. from the results of a cross-linking experiment, the pli was found to present as a homotrimer of the subunit. the fundamental properties of a. bl ...19938514730
purification and primary structure of a myotoxic lysine-49 phospholipase a2 with low lipolytic activity from trimeresurus gramineus venom.four acidic phospholipase a2 (pla2) isozymes named pla2-i, ii, iii and iv have previously been isolated from trimeresurus gramineus (green habu snake) venom and sequenced [oda et al. (1991) toxicon 29, 157; fukagawa et al. (1992) toxicon 30, 1131; fukagawa et al. (1993) toxicon 31, 957]. they contain aspartate-49 which is known to bind ca2+, essential for catalysis. in the present study, a basic pla2 named pla2-v containing lysine-49 was newly isolated from the same snake venom. its isoelectric ...19958744986
amino acid sequence of a lectin-like protein from lachesis muta stenophyrs venom.the primary structure of the lectin-like protein from lachesis muta stenophyrs venom was deduced from analysis of the n-terminus and the sequence of peptides obtained after digestion with trypsin, arg-c enzyme, staphylococcus aureus v8 protease and endoproteinase asp-n. peptides generated by cleavage of the lectin with cyanogen bromide and o-iodosobenzoic acid were also sequenced. comparison of the complete 135 amino acid residues sequence with those of the lectin from the venom of crotalus atro ...19968843577
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