Characterization of Ac1-Proteinase from the venom of Agkistrodon acutus (Hundred-pace snake) from Taiwan.
1. Ac1-Proteinase from the venom of Agkistrodon acutus was isolated in a homogeneous form by a previously published method. 2. Ac1-Proteinase possessed lethal, hemorrhagic, caseinolytic, azocaseinolytic, azoalbumin hydrolytic and hide powder azure hydrolytic activities. 3. The toxin also hydrolyzed the oxidized B chain of insulin and fibrinogen. The cleavage sites in the oxidized B chain of insulin were identified as Ala(14)-Leu(15) and Tyr(16)-Leu(17). The A alpha chain of fibrinogen was digested. 4. Biological properties of Ac1-Proteinase were investigated further and are reported in this paper.
Nikai
T
T
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
Kato
C
C
Komori
Y
Y
Sugihara
H
H
Homma
M
M
D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000032:analysis*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism* / Q000633:toxicity; D005340:Fibrinogen / Q000378:metabolism; D006470:Hemorrhage / Q000139:chemically induced; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism; D051379:Mice; D008813:Mice, Inbred ICR; D008969:Molecular Sequence Data; D009132:Muscles / Q000473:pathology; D009135:Muscular Diseases / Q000139:chemically induced; D009336:Necrosis / Q000139:chemically induced; D010446:Peptide Fragments / Q000378:metabolism; D013379:Substrate Specificity
C031442:Agkistrodon venoms; D003435:Crotalid Venoms; D007328:Insulin; D010446:Peptide Fragments; D005340:Fibrinogen; D010450:Endopeptidases; C039589:Ac1-proteinase