A double headed serine proteinase inhibitor--human plasma kallikrein and elastase inhibitor--from Boophilus microplus larvae.
Immunopharmacology
; 45(1-3): 171-7, 1999 Dec.
Article
em En
| MEDLINE
| ID: mdl-10615008
ABSTRACT
Preying on cattle, the hard tick Boophilus microplus causes heavy economical losses to Brazil. Tick proteins are a good target to be used as tools for tick control. Serine protease inhibitors from B. microplus larvae (BmTI) were preliminarily characterized. One-week-old larvae were the source of a 2% protein solution in 5 mM Tris-HCl, 20 mM NaCl, pH 7.4. The inhibitors were purified by affinity chromatography on trypsin-Sepharose, and ion-exchange chromatography on Resource Q column, and they separated in two major active peaks, corresponding to 10-kDa and 18-kDa proteins (BmTI-B and BmTI-A, respectively). Both purified proteins inhibited trypsin with Ki of 0.3 and 3.0 nM, respectively, but only the 18-kDa protein inhibited elastase (Ki 1.4 nM) and plasma kallikrein (Ki 120 nM). BmTI-A did not change prothrombin time (PT) and thrombin time (TT), but it increased activated partial thromboplastin time (APTT) was dose-dependent. The partial amino acid sequence indicated that BmTI-A belongs to the bovine pancreatic trypsin inhibitor (BPTI)-Kunitz type inhibitor family. These inhibitors (by their properties) play a role in the feeding process of the tick. Development of antibodies against these proteins may be used to impair the normal feeding and consequently, the parasite would be no longer viable.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Carrapatos
/
Calicreínas
/
Elastase Pancreática
/
Inibidores de Serina Proteinase
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Immunopharmacology
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
HOLANDA
/
HOLLAND
/
NETHERLANDS
/
NL
/
PAISES BAJOS
/
THE NETHERLANDS