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pubmed-article:3360144pubmed:abstractTextA method of the covalent immobilization of proteins on the surface of liposomes, containing 10% (by mol) of N-glutaryl phosphatidylethanolamine, is described. Carboxylic groups of liposomal N-glutaryl phosphatidylethanolamine were activated in the presence of water-soluble carbodiimide and N-hydroxysulfosuccinimide and reacted subsequently with protein amino groups. The liposome-protein conjugates formed contained up to 5 x 10(-4) mol protein/mol lipid. Lectins (RCA1 and WGA) upon immobilization on liposomes retained saccharide specificity and the ability to agglutinate red blood cells. The immobilization of mouse monoclonal IgG in a ratio of 3.5 x 10(-4) mol IgG/mol lipid was achieved. The liposome activation in the absence of N-hydroxysulfosuccinimide resulted in a 2-fold decrease of protein coupling yields.lld:pubmed
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pubmed-article:3360144pubmed:dateRevised2001-3-23lld:pubmed
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pubmed-article:3360144pubmed:articleTitleProtein immobilization on the surface of liposomes via carbodiimide activation in the presence of N-hydroxysulfosuccinimide.lld:pubmed
pubmed-article:3360144pubmed:affiliationUSSR Cardiology Research Center, Academy of Medical Sciences, Moscow.lld:pubmed
pubmed-article:3360144pubmed:publicationTypeJournal Articlelld:pubmed
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