Purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of horn fly, Haematobia irritans irritans (Diptera: Muscidae).
J Protein Chem
; 19(6): 515-21, 2000 Aug.
Article
em En
| MEDLINE
| ID: mdl-11195976
This work describes the purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of Haematobia irritans irritans (Diptera: Muscidae). The enzyme was purified using a one-step process, consisting of affinity chromatography on SBTI-Sepharose. The purified protease showed one major active proteinase band on reverse zymography with 0.15% gelatin, corresponding to a molecular mass of 25.5 kDa, with maximum activity at pH 9.0. The purified trypsin-like enzyme preferentially hydrolyzed synthetic substrates with arginine residue at the P1 position. The Km values determined for three different substrates were 1.88 x 10(-4), 1.28 x 10(-4), and 1.40 x 10(-4) M for H-alpha-benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide (S2222), DL-Ile-Pro-Arg-p-nitroanilide (S2288), and DL-Phe-Pip-Arg-p-nitroanilide (S2238), respectively. The enzyme was strongly inhibited by typical serine proteinase inhibitors such as SB
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Muscidae
/
Serina Endopeptidases
/
Fibrinolíticos
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Protein Chem
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Estados Unidos