Flavorase, a novel non-haemorrhagic metalloproteinase in Protobothrops flavoviridis venom, is a target molecule of small serum protein-3.
J Biochem
; 158(1): 37-48, 2015 Jul.
Article
en En
| MEDLINE
| ID: mdl-25681613
Some venomous snakes possess anti-toxic proteins in their sera that may play a role in neutralizing the haemorrhagic factors or toxins in their own venom. Five small serum proteins (SSP-1-SSP-5) were isolated from the serum of Japanese viper (Protobothrops flavoviridis), and were found to act as self-defence proteins against the viper's own toxic components. However, the physiological function of SSP-3 has not been completely elucidated. Affinity chromatography of the venom on an SSP-3-immobilized column identified a novel 55-kDa protein as the target molecule of SSP-3. Sequences of internal fragments of this SSP-3-binding protein showed high homology to those of metalloproteinases from the P. flavoviridis venom. The cDNA sequence revealed that this protein, termed flavorase, is a P-III class metalloproteinase consisting of 423 amino acid residues. The purified protein did not show haemorrhagic and cytotoxic activity. Biacore measurements revealed that SSP-3 was bound to flavorase with a dissociation constant of 6.4 × 10(-9) M. SSP-3 non-competitively inhibited the peptidase activity of flavorase with an inhibition constant of 6.6 × 10(-9) M.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Venenos de Serpiente
/
Proteína 3 de Unión a Factor de Crecimiento Similar a la Insulina
/
Metaloproteasas
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Biochem
Año:
2015
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Reino Unido