{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,6,24]],"date-time":"2024-06-24T02:10:23Z","timestamp":1719195023105},"reference-count":29,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":8070,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motility"],"published-print":{"date-parts":[[1983,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Further similarity between mammalian erythrocyte spectrin and pig brain spectrin has been demonstrated by (a) formation of hybrid molecules with brain \u03b1\u2010chains and erythrocyte \u03b2\u2010chains and by (b) identification of an ankyrin protein in brain membranes. Hybrid spectrin molecules prepared from brain \u03b1\u2010chains and erythrocyte \u03b2\u2010chains were visualized by low\u2010angle rotary shadowing as double\u2010stranded rods (dimers) 100 nM in length. <jats:sup>125<\/jats:sup>I\u2010labeled brain \u03b1\u2010chain that was hybridized with erythrocyte \u03b2\u2010subunit acquired ability to bind to ankyrin sites on erythrocyte membranes. <jats:sup>125<\/jats:sup>I\u2010labeled brain \u03b1\u2010chain bound only to \u03b2\u2010subunits of erythrocyte and brain spectrin following transfer of these polypeptides to nitrocellulose paper from sodium dodecyl sulfate (SDS) gels. Thus brain spectrin and mammalian erythrocyte spectrin have shared functional sites involved in association of their subunits. Additional evidence for similarity of brain and erythrocyte membranes is the finding of a 210,000 <jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub> membrane protein in brain that cross\u2010reacts with erythrocyte ankyrin and has a water\u2010soluble domain of 72,000 <jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub> that is produced by protease digestion. The 72,000 <jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub> domain of brain ankyrin has been isolated by affinity chromatography on erythrocyte spectrin\u2010Sepharose, and was demonstrated to bind directly to erythrocyte and brain spectrin. The brain 72,000 <jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub> fragment has distinct peptide maps from the erythrocyte 72,000 <jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub> ankyrin fragment and thus is not a result of erythrocyte contamination.<\/jats:p>","DOI":"10.1002\/cm.970030527","type":"journal-article","created":{"date-parts":[[2005,4,11]],"date-time":"2005-04-11T19:33:39Z","timestamp":1113248019000},"page":"623-633","source":"Crossref","is-referenced-by-count":6,"title":["Spectrin and ankyrin in brain"],"prefix":"10.1002","volume":"3","author":[{"given":"Vann","family":"Benett","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan","family":"Davis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.95.1.278"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"2292","DOI":"10.1016\/S0021-9258(17)38072-9","article-title":"Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin","volume":"253","author":"Bennett V.","year":"1978","journal-title":"J. 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