Antihemorrhagin in the blood serum of king cobra (Ophiophagus hannah): purification and characterization.
King cobra (Ophiophagus hannah) serum was found to possess antihemorrhagic activity against king cobra hemorrhagin. The activity was stronger than that in commercial king cobra antivenom. An antihemorrhagin has been purified by ion exchange chromatography, affinity chromatography and gel filtration with a 22-fold purification and an overall yield of 12% of the total antihemorrhagic activity contained in crude serum. The purified antihemorrhagin was homogeneous in disc-PAGE and SDS-PAGE. Its apparent molecular weight determined by SDS-PAGE was 120 kDa. The antihemorrhagin was also active against other hemorrhagic snake venoms obtained in Thailand and Japan such as Calloselasma rhodostoma, Trimeresurus albolabris, Trimeresurus macrops and Trimeresurus flavoviridis (Japanese Habu). It inhibited the proteolytic activity of king cobra venom. It is an acid- and thermolabile protein and does not form precipitin lines against king cobra venom.
Chanhome
Lawan
L
Queen Saovabha Memorial Institute, Thai Red Cross Society, 1871 Rama IV Rd., 10330, Bangkok, Thailand
Khow
Orawan
O
Omori-Satoh
Tamotsu
T
Sitprija
Visith
V
D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D017815:Elapidae / Q000097:blood*; D010450:Endopeptidases / Q000187:drug effects / Q000378:metabolism; D006470:Hemorrhage / Q000188:drug therapy*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011817:Rabbits; D012910:Snake Venoms / Q000378:metabolism
D001798:Blood Proteins; D012910:Snake Venoms; C003941:antihemorrhagic factor; D010450:Endopeptidases; C041605:hemorrhagic proteinase IV