Reevaluation of hemorrhagic toxin, HR-I, from Agkistrodon halys blomhoffii venom: proof of proteolytic enzyme.
HR-I is a hemorrhagic toxin originally isolated from Agkistrodon halys blomhoffii (Mamushi) venom by Oshima et al. (1972). It was reported by the original investigators that it was nonproteolytic when casein was used as the substrate. HR-I was isolated again and proteolytic activity was tested using different substrates and assay methods. It is shown that HR-I is indeed a proteolytic enzyme hydrolyzing a number of peptide bonds. This present investigation suggests that more than one method should be used for proteolytic enzyme assay of hemorrhagic toxins. Toxicological and biochemical properties of HR-I were further investigated and are reported in this paper.
Nikai
T
T
Oguri
E
E
Kishida
M
M
Sugihara
H
H
Mori
N
N
Tu
A T
AT
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003435:Crotalid Venoms / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity; D006470:Hemorrhage / Q000139:chemically induced; D005779:Immunodiffusion; D051379:Mice; D008970:Molecular Weight; D009928:Organ Specificity; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D013379:Substrate Specificity
D000596:Amino Acids; D003435:Crotalid Venoms; D010446:Peptide Fragments; C032814:hemorrhagin components (Crotalid); D010447:Peptide Hydrolases