{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T09:17:35Z","timestamp":1787563055863,"version":"build-2736575974"},"reference-count":47,"publisher":"Canadian Science Publishing","issue":"5","license":[{"start":{"date-parts":[[1996,9,1]],"date-time":"1996-09-01T00:00:00Z","timestamp":841536000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochem. Cell Biol."],"published-print":{"date-parts":[[1996,9,1]]},"abstract":"<jats:p>\n                    Calgizzarin is a Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding protein of the S100 family that has been implicated in the regulation of cytoskeletal function through its Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent interaction with annexin I. The Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding properties of calgizzarin (S100C) have not previously been thoroughly characterized. Calgizzarin, therefore, was purified from chicken gizzard smooth muscle by exploiting its Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent interaction with the hydrophobic matrix phenyl-Sepharose and is shown by\n                    <jats:sup>45<\/jats:sup>\n                    Ca\n                    <jats:sup>2+<\/jats:sup>\n                    overlay to bind Ca\n                    <jats:sup>2+<\/jats:sup>\n                    more weakly than does calmodulin. Gel filtration in the absence and presence of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    suggested a dimeric structure of calgizzarin and indicated a more compact structure in the presence of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    . Flow dialysis experiments indicated that, at physiological ionic strength, calgizzarin binds two Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ions per monomer (four per native dimer), as predicted from the deduced amino acid sequence which contains two putative EF-hands, with [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>0.5<\/jats:sub>\n                    of 0.52\u2002mM and n\n                    <jats:sub>H<\/jats:sub>\n                    of 1.4\u2002in the absence of Mg\n                    <jats:sup>2+<\/jats:sup>\n                    and [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>0.5<\/jats:sub>\n                    of 0.3\u2002mM and n\n                    <jats:sub>H<\/jats:sub>\n                    of 1.2\u2002in the presence of 10\u2002mM MgCl\n                    <jats:sub>2<\/jats:sub>\n                    . The hydrophobic fluorescent probe 2-p-toluidinylnaphthalene-6-sulphonate was used to demonstrate Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent exposure of a hydrophobic site(s) in calgizzarin. This approach also indicated the ability of calgizzarin to bind Zn\n                    <jats:sup>2+<\/jats:sup>\n                    . Interestingly, the affinity of calgizzarin for Ca\n                    <jats:sup>2+<\/jats:sup>\n                    was enhanced approximately 10-fold in the presence of the hydrophobic probe, possibly reflecting an increased affinity for Ca\n                    <jats:sup>2+<\/jats:sup>\n                    when calgizzarin binds to a target protein. Finally, the distribution of calgizzarin among chicken tissues was examined by immunoblotting: calgizzarin was expressed at its highest levels in lung tissue, followed by smooth muscle tissues (oesophagus, large intestine, trachea, and gizzard), kidney, liver, brain, and heart; it was not detected in small intestine or skeletal muscle.Key words: calcium-binding protein, calgizzarin, S100C, smooth muscle, zinc.\n                  <\/jats:p>","DOI":"10.1139\/o96-075","type":"journal-article","created":{"date-parts":[[2009,12,23]],"date-time":"2009-12-23T14:51:40Z","timestamp":1261579900000},"page":"687-694","source":"Crossref","is-referenced-by-count":30,"title":["Characterization of the Ca\n                    <sup>2+<\/sup>\n                    -binding properties of calgizzarin (S100C) isolated from chicken gizzard smooth muscle"],"prefix":"10.1139","volume":"74","author":[{"given":"Bruce G.","family":"Allen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael P.","family":"Walsh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Durussel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos A.","family":"Cox","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"155","reference":[{"key":"p_1\/p_1_1","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/0968-0004(94)90112-0","volume":"19","author":"Allen B.G.","year":"1994","journal-title":"Trends Biochem. 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