BmSI-7, a novel subtilisin inhibitor from Boophilus microplus, with activity toward Pr1 proteases from the fungus Metarhizium anisopliae
Data
2008-02-01
Autores
Sasaki, Sergio D. 
Lima, Cdssia A. de
Lovato, Diogo V.
Juliano, Maria A.
Torquato, Ricardo J. S.
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BmSI-7 and BmSI-6, two Boophilus microplus subtilisin inhibitors (BmSI) were purified and characterized from eggs. the inhibitors isolated by classical purification methods presented molecular masses of 7408 and 7271 Da, respectively, by MALDI-TOF-MS. Both BmSI-7 and BmSI-6 inhibited neutrophil elastase (K-i 0.4 and 0.3 nM) and subtilisin A (K-i 1.4 nM for both inhibitors). They also strongly inhibited Pr1 proteases from the fungus Metarhizium anisopliae; BmSI-7 (K-i 50 nM) and BmSI-6 (K-i 2.2 nM). the BmSI-7 full length cDNA was obtained using amino acid sequence information of BmSI-7 peptides generated by proteolytic digestion. BmSI-7 belongs to trypsin inhibitor like cysteine rich domain family (TIL), and it is transcribed in ovary, fat body, gut, salivary gland and haemocytes. BmSI-7 is the first TIL inhibitor described with inhibitory activity toward subtilisin A and Pr1 proteases of entomopathogenic fungi. (C) 2007 Elsevier Inc. All rights reserved.
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Experimental Parasitology. San Diego: Academic Press Inc Elsevier Science, v. 118, n. 2, p. 214-220, 2008.