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| Varenne, A; Gareil, P; Colliec-jouault, Sylvia; Daniel, R. |
| The interaction of proteins with polysaccharides represents a major and challenging topic in glycobiology, since such complexes mediate fundamental biological mechanisms. An affinity capillary electrophoresis method has been developed to evidence the complex formation and to determine the binding properties between an anticoagulant polysaccharide of marine origin, fucoidan, and a potential target protein, antithrombin. This method is a variant of zonal electrophoresis in the mobility shift format. A fixed amount of protein was injected into a capillary filled with a background electrolyte containing the polysaccharide in varying concentrations. The effective mobility data of the protein were processed according to classical linearization treatments to... |
| Tipo: Text |
Palavras-chave: Antithrombin; Fucoidan; Electrophoresis; Protein interaction; Polysaccharides. |
| Ano: 2003 |
URL: http://archimer.ifremer.fr/doc/2003/publication-2114.pdf |
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| Gozzo,A.J.; Nunes,V.A.; Nader,H.B.; Dietrich,C.P.; Carmona,A.K.; Sampaio,M.U.; Sampaio,C.A.M.; Araújo,M.S.. |
| Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Glycosaminoglycans; Human plasma kallikrein; Plasminogen; Factor XII; C1-inhibitor; Antithrombin. |
| Ano: 2003 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000800011 |
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| Yang,L.; Manithody,C.; Rezaie,A.R.. |
| We recently demonstrated that the substitution of the autolysis loop (residues 143 to 154 in the chymotrypsin numbering system) of activated protein C (APC) with the corresponding loop of factor Xa (fXa) renders the APC mutant (APC/fX143-154) susceptible to inhibition by antithrombin (AT) in the presence of pentasaccharide. Our recent results further indicated, that in addition to an improvement in the reactivity of APC/fX143-154 with AT, both the amidolytic and anti-factor Va activities of the mutant APC have also been significantly increased. Since the autolysis loop of APC is five residues longer than the autolysis loop of fXa, it could not be ascertained whether this loop in the mutant APC specifically interacts with the activated conformation of AT or... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Activated protein C; Factor Va; Antithrombin; Factor Xa; Serpins. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007000800005 |
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