Purification and partial characterization of a new pro-inflammatory lectin from Bauhinia bauhinioides Mart (Caesalpinoideae) seeds.

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 Lett

authors

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 BS

doi

10.2174/092986611794653987

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

396-402

issue

4

eissn

0929-8665

issn

1875-5305

pii

BSP/ PPL/ E pub/0252

journal_volume

18

pub_type

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