{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,15]],"date-time":"2025-12-15T13:49:13Z","timestamp":1765806553018},"reference-count":46,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[2006,6,29]],"date-time":"2006-06-29T00:00:00Z","timestamp":1151539200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2006,7]]},"abstract":"<jats:p>Annexin\u2003B1 from <jats:italic>Cysticercus cellulosae<\/jats:italic> has recently been identified using immunological screening in an attempt to find novel antigens for vaccine development against cysticercosis. The protein possesses anticoagulant activity and carries significant therapeutic potential due to its thrombus\u2010targeting and thrombolytic properties. We investigated the biochemical properties of annexin\u2003B1 using liposome and heparin Sepharose copelleting assays, as well as CD spectroscopy. The calcium\u2010dependent binding to acidic phospholipid membranes is reminiscent of other mammalian annexins with a clear preference for high phosphatidylserine content. A unique property of annexin\u2003B1 is its ability to bind to liposomes with high phosphatidylserine content in the absence of calcium, which might be due to the presence of several basic residues on the convex protein surface that harbours the membrane\u2010binding loops. Annexin\u2003B1 demonstrates lectin properties and binds to heparin Sepharose in a cooperative, calcium\u2010dependent manner. Although this binding is reversible to a large extent, a small fraction of the protein remains bound to the glycosaminoglycan even in the presence of high concentrations of EDTA. Analogous to annexin\u2003A5, we propose a model of heparin wrapped around the protein thereby engaging in calcium\u2010dependent and calcium\u2010independent interactions. Although the calcium\u2010independent heparin\u2010binding sites identified in annexin\u2003A5 are not conserved, we hypothesize three possible sites in annexin\u2003B1. Results from CD spectroscopy and thermal denaturation indicate that, in solution, the protein binds calcium with a low affinity that leads to a slight increase in folding stability.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05332.x","type":"journal-article","created":{"date-parts":[[2006,6,30]],"date-time":"2006-06-30T09:33:31Z","timestamp":1151660011000},"page":"3238-3247","source":"Crossref","is-referenced-by-count":16,"title":["Biochemical characterization of annexin B1 from <i>Cysticercus cellulosae<\/i>"],"prefix":"10.1111","volume":"273","author":[{"given":"Anja","family":"Winter","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adlina 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