| characterization, primary structure and molecular evolution of anticoagulant protein from agkistrodon actus venom. | an anticoagulant protein named aaacp was isolated from agkistrodon actus (hundred-pace snake of taiwan, viperidae) venom. aaacp inhibited the factor xa-induced plasma coagulation in a concentration-dependent manner. thus, aaacp seems to bind to factor xa in prothrombinase complex. aaacp was composed of a and b chains linked by disulphide bond(s). the amino acid sequences of a and b chains of aaacp were analysed with a few residues unidentified which were complemented from the nucleotide sequence ... | 2002 | 12175618 |
| treatment of poisonous snakebites in northern taiwan. | we evaluated the epidemiology and outcomes of snakebites in northern taiwan, and the effect of local antivenom injection to speed neutralization and reduce the spread of venom. | 2000 | 10770028 |
| the relationship between the dose of taiwan cobra (naja atra) and taiwan habu (trimeresurus mucrosquamatus) venom and time of death in mice. | | 1956 | 13357745 |
| management of poisonous snake bites in southern taiwan. | snake bite envenomation is not uncommon in taiwan. this study focuses on the pattern of poisonous snake bites and their management in southern taiwan over a 5-year period. the case histories of 37 patients with poisonous snake bites admitted to the kaohsiung medical university hospital between june 2001 and july 2005 were analyzed retrospectively. three patients, bitten by unknown species of venomous snakes, were excluded from this study. the frequency of snakebites from each species of snake, t ... | 2007 | 18055297 |
| isolation of a venom factor devoid of proteolytic activity from taiwan habu (trimeresurus mucrosquamatus): n-terminal sequence homology and no functional similarity to factors ix/x-binding proteins and botrocetin. | one novel venom factor was isolated and purified from the venom of taiwan habu (trimeresurus mucrosquamatus) using two consecutive anion-exchange and gel-filtration chromatographies followed by cation-exchange hplc. further characterization of the purified protein indicated that it lacks the proteolytic activity toward fibrinogen molecules, suggesting that this protein factor does not belong to the familes of metalloproteinases and thrombin-like serine proteases commonly found in the crude venom ... | 1996 | 8968958 |