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Type: Artigo de periódico
Title: Isolation And Characterization Of A Lectin-like Protein From Bothhops Jararacüssv Venom
Author: Carvalho D.D.
Marangon S.
Oilvelra D.
Novklo J.C.
Abstract: Lectin-like proteins have been found In the venom of Elapidae, Viperidae and Crotalidae snakes. These proteins hind to lactose moieties and induce agglutination of erythrocytes. aggregation of platelets and are mitogenic to Ivinphocytes. A galactose-sperific lectin in Hothrops jarararussu venom (BJcuL) was adsorbed on a immobilized D-galactose column and eluted with 0.1 M lactose. On SDS-PACE (reducing conditions - (UM DTT). the fraction eluted showed a single band of 15 kDa, and under non-reducing conditions, a major band of 30 kDa. Trypsined erythrocytes from pig and cow were agglutinated by B.IcuL. with end points of 0.5 and 2.0 //g/ml, respectively. The hemagglutination of trypsined pig erythrocytes induced by '1.0 g/rnl of BJcuI. was inhibited specifically in the presence of 0.8 m M lactose, .'i.2 mM galactose. 3.2 m M raffinose, 0.2 mM EI) TA or 0.1 m M EGTA. The association of subunit s via interchain dissulfide bonds is essencial for lectin activity, since DTT-reduced BJcuL showed no hemagglutination activity against pig erythrocytes. Reduced and S-pyridylethylated B.IcuL (RP-B.JcuL) was separated as a single peak by reverse-phase BPLC on a (-18/Bondapack column. The preliminary results showed that BJcuL have a single \-terminal amino acid sequence on sequencer analysis, indicating that B.IcuL is a homodimer. The X-terrninal 4-residue, NNCP, shows homology with others lectins from snake venoms BJL, HSI. and LmsL. Experiments are in progress to determine the rest of N-termirial sequence.
Rights: fechado
Identifier DOI: 
Date Issue: 1997
Appears in Collections:Unicamp - Artigos e Outros Documentos

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