Abstract:
:A new galactose-specific lectin, named BBL, was purified from seeds of Bauhinia bauhinioides by precipitation with ammonium sulfate, followed by two steps of ion exchange chromatography. BBL haemagglutinated rabbit erythrocytes (native and treated with proteolytic enzymes) showing stability even after exposure to 60 °C for an hour. The lectin haemagglutinating activity was optimum between pH 8.0 and 9.0 and inhibited after incubation with D-galactose and its derivatives, especially α-methyl-D-galactopyranoside. The pure protein possessed a molecular mass of 31 kDa by SDS-PAGE and 28.310 Da by mass spectrometry. The lectin pro-inflammatory activity was also evaluated. The s.c. injection of BBL into rats induced a dose-dependent paw edema, an effect that occurred via carbohydrate site interaction and was significantly reduced by L-NAME, suggesting an important participation of nitric oxide in the late phase of the edema. These findings indicate that BBL can be used as a tool to better understand the mechanisms involved in inflammatory responses.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Silva HC,Bari AU,Pereira-Jénior FN,Simões RC,Barroso-Neto IL,Nobre CB,Pereira MG,Nascimento KS,Rocha BA,Delatorre P,Nagano CS,Assreuy AM,Cavada BSdoi
10.2174/092986611794653987subject
Has Abstractpub_date
2011-04-01 00:00:00pages
396-402issue
4eissn
0929-8665issn
1875-5305pii
BSP/ PPL/ E pub/0252journal_volume
18pub_type
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