Interaction of diocleinae lectins with glycoproteins based in surface plasmon resonance
Mem. Inst. Oswaldo Cruz
;
97(2): 275-279, Mar. 2002. ilus, graf
Artigo
em Inglês
| LILACS
| ID: lil-326293
ABSTRACT
Interaction of glucose/mannose-binding lectins in solution with immobilized glycoproteins was followed in real time using surface plasmon resonance technology. The lectins which share many biochemical and structural features could be clearly differentiated in terms of their specificity for complex glycoconjugates. The most prominent interaction of the lectins with PHA-E comparing with soybean agglutinin, both glycoproteins exhibiting high mannose oligosaccharides, suggests that the whole structure of the glycoproteins themselves, may interfere in affinity. These findings also support the hypothesis that minor amino acid replacements in the primary sequence of the lectins might be responsible for their divergence in fine specificity and biological activities. This is the first report using surface plasmon resonance technology that evidences differences of Diocleinae lectins in respect their fine glycan-specificity
Texto completo:
DisponíveL
Índice:
LILACS (Américas)
Assunto principal:
Glicoproteínas
Idioma:
Inglês
Revista:
Mem. Inst. Oswaldo Cruz
Assunto da revista:
Medicina Tropical
/
Parasitologia
Ano de publicação:
2002
Tipo de documento:
Artigo
País de afiliação:
Brasil
/
França
Instituição/País de afiliação:
Faculté des Sciences Pharmaceutiques/FR
/
Universidade Federal do Ceará/BR
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