title: Isolation and characterization of a hemorrhagin from the venom of Calloselasma rhodostoma (Malayan pit viper).
abstract: The major hemorrhagin (termed rhodostoxin) of the venom of Calloselasma rhodostoma (Malayan pit viper) was purified to electrophoretic homogeneity by Sephadex G-200 gel filtration followed by high performance ion exchange chromatography. The purified hemorrhagin also yielded a single peak in reversed-phase HPLC. It had an isoelectric point of 5.3 and a mol. wt of 34,000. Rhodostoxin exhibited potent proteolytic, hemorrhagic and edema-inducing activities but was not lethal to mice at a dose of 6 microgram/g (i.v.). Treatment of rhodostoxin with EDTA eliminated both the proteolytic and hemorrhagic activities completely. The N-terminal sequence of rhodostoxin was determined to be NHEIKRHVDIVVVXDSRFCTK.
authors.affiliation: Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.
authors.forename: G
authors.initials: G
authors.lastname: Ponnudurai
authors.forename: M C
authors.initials: MC
authors.lastname: Chung
authors.forename: N H
authors.initials: NH
authors.lastname: Tan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000633:toxicity; D004487:Edema / Q000139:chemically induced; D051379:Mice; D008969:Molecular Sequence Data
chemical_list: D003435:Crotalid Venoms