Purification of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi).
Toxicon
; 31(10): 1213-9, 1993 Oct.
Article
em En
| MEDLINE
| ID: mdl-8303715
ABSTRACT
A capillary permeability-increasing enzyme-2 was purified from the venom of A. caliginosus by ion-exchange chromatography and gel filtration on Sephadex G-100. By this procedure, 3.1 mg of purified enzyme was obtained from 4 g of the venom. The mol. wt of the purified enzyme was estimated to be approximately 44,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme hydrolyzed N-alpha-tosyl-L-arginine methylester with a specific activity of 56.5 units/mg of protein, and did not show any caseinolytic, clotting or bradykinin-releasing activity. When 13.9 micrograms of the enzyme was injected into the depilated skin on the back of a rabbit, capillary permeability was increased.
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Base de dados:
MEDLINE
Assunto principal:
Permeabilidade Capilar
/
Serina Endopeptidases
/
Hidrolases de Éster Carboxílico
/
Agkistrodon
/
Venenos de Crotalídeos
Idioma:
En
Ano de publicação:
1993
Tipo de documento:
Article
País de afiliação:
Japão