A novel serine protease from pseuderanthemum latifolium B. Hansen: Characterization and fibrino(geno)lytic activities.
Nat Prod Res
; 35(16): 2640-2646, 2021 Aug.
Article
em En
| MEDLINE
| ID: mdl-31441669
ABSTRACT
Protease (PPL) was isolated from Pseuderanthemum latifolium B. Hansen and had a molecular mass of 70 kDa. The N-terminal sequence of PPL showed 70-80% similarity with of subtilisin-like serine proteases from plants, but it did not show any sequence homology with known plant proteases. Serine protease inhibitors (PMSF, DFP) effectively blocked about 90% of PPL activity. PPL was highly activity at the pH range from 6 to 9 and temperatures from 50 °C to 80 °C, with an optimum at pH 7.0 and temperatures 70 °C. PPL had stability in a variety of pH, temperature, surfactant and oxidizing agents. PPL with concentration of 2.5 µg completely hydrolyzed the Aα-chain of fibrinogen within 5 min and hydrolyzed the Bß and the γ-chain after 10 h. Fibrin also was strong hydrolyzed by PPL with concentration of 0.3 µg. Thus, PPL is a unique serine protease, which it had strong fibrino(geno)lytic activities.
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Tema:
Geral
Bases de dados:
MEDLINE
Assunto principal:
Acanthaceae
/
Serina Proteases
Idioma:
En
Revista:
Nat Prod Res
Ano de publicação:
2021
Tipo de documento:
Article