Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase

Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase

Autor Lima, VLM Google Scholar
Correia, MTS Google Scholar
Cechinel, YMN Google Scholar
Sampaio, CAM Google Scholar
Owen, J. S. Google Scholar
Coelho, LCBB Google Scholar
Instituição UNIV LONDON
Universidade Federal de Pernambuco (UFPE)
Universidade Federal de São Paulo (UNIFESP)
Resumo A crude seed extract from the native Brazilian forage, Cratylia mollis Mart., and its purified lectin (termed Cra), were found to precipitate glycoproteins from serum. An affinity column of Cra lectin coupled to Sepharose CL-4B was prepared and its ability to isolate glycoproteins from human plasma compared to that of a commercial immobilized lectin, Concanavalin (Con) A-Sepharose. Although both lectins are of the alpha-D-mannose/alpha-D-glucose binding class, clear differences in the type and amount of serum glycoproteins adsorbed were seen on analysis by denaturing polyacrylamide gel electrophoresis. Similarly, when a semipurified preparation of the plasma glycoprotein, lecithin-cholesterol acyltransferase (LCAT, EC 2.3.1.43) was applied to the columns some differences were evident; most LCAT was not retained by either matrix but when the bound fractions were eluted and analyzed electrophoretically the LCAT isolated by the Cra-Sepharose column was much purer. These findings suggest that immobilized Cra lectin has the potential for use in studies both to isolate and to characterize certain serum glycoproteins. (C) 1997 Elsevier B.V.
Idioma Inglês
Data de publicação 1997-05-01
Publicado em Carbohydrate Polymers. Oxford: Elsevier B.V., v. 33, n. 1, p. 27-32, 1997.
ISSN 0144-8617 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 27-32
Fonte http://dx.doi.org/10.1016/S0144-8617(97)00034-9
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1997XM81700005
Endereço permanente http://repositorio.unifesp.br/handle/11600/25719

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