New insights on the specificity of heparin and heparan sulfate lyases from Flavobacterium heparinum revealed by the use of synthetic derivatives of K5 polysaccharide from E-coli and 2-O-desulfated heparin

New insights on the specificity of heparin and heparan sulfate lyases from Flavobacterium heparinum revealed by the use of synthetic derivatives of K5 polysaccharide from E-coli and 2-O-desulfated heparin

Autor Nader, H. B. Google Scholar
Kobayashi, E. Y. Google Scholar
Chavante, S. F. Google Scholar
Tersariol, ILS Google Scholar
Castro, RAB Google Scholar
Shinjo, S. K. Google Scholar
Naggi, A. Google Scholar
Torri, G. Google Scholar
Casu, B. Google Scholar
Dietrich, C. P. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
UFRN
Ist Chim & Biochim G Ronzoni
Resumo The capsular polysaccharide from E. Coli, strain K5 composed of ....--> 4)beta-D-GlcA(1 --> 4)alpha-D-GlcNAc(1 --> 4)beta-D-GlcA (1 -->....., chemically modified K5 polysaccharides, bearing sulfates at C-2 and C-6 of the hexosamine moiety and at the C-2 of the glucuronic acid residues as well as 2-O desulfated heparin were used as substrates to study the specificity of heparitinases I and II and heparinase from Flavobacterium heparinum. the natural K5 polysaccharide was susceptible only to heparitinase I forming Delta U-GlcNAc. N-deacetylated, N-sulfated K5 became susceptible to both heparitinases I and II producing Delta U-GlcNS. the K5 polysaccharides containing sulfate at the C-2 and C-6 positions of the hexosamine moiety and C-2 position of the glucuronic acid residues were susceptible only to heparitinase II producing Delta U-GlcNS,6S and Delta U,2S-GlcNS,6S respectively. These combined results led to the conclusion that the sulfate at C-6 position of the glucosamine is impeditive for the action of heparitinase I and that heparitinase II requires at least a C-2 or a C-6 sulfate in the glucosamine residues of the substrate for its activity. Iduronic acid-2-O-desulfated heparin was susceptible only to heparitinase II producing Delta U-GlcNS,6S. All the modified K5 polysaccharides as well as the desulfated heparin were not substrates for heparinase. This led to the conclusion that heparitinase II acts upon linkages containing non-sulfated iduronic acid residues and that heparinase requires C-2 sulfated iduronic acid residues for its activity.
Palavra-chave heparan sulfate lyases, specificity
heparinase, specificity
sulfated K5 polysaccharides
heparan sulfate, structure
Idioma Inglês
Data de publicação 1999-06-01
Publicado em Glycoconjugate Journal. Dordrecht: Kluwer Academic Publ, v. 16, n. 6, p. 265-270, 1999.
ISSN 0282-0080 (Sherpa/Romeo, fator de impacto)
Publicador Kluwer Academic Publ
Extensão 265-270
Fonte http://dx.doi.org/10.1023/A:1007057826179
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000082733500002
Endereço permanente http://repositorio.unifesp.br/handle/11600/26091

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