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. 2000 Nov 27;151(5):985–1002. doi: 10.1083/jcb.151.5.985

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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(A) Western blotting with the affinity-purified antibody against a COOH-terminal peptide of βIV spectrin (βIV-CT) on 50 μg protein from rat brain PNS (brain, lanes 1 and 3) and homogenates of human pancreatic islets (islets, lanes 2 and 4). In the case of islets, the βIV-CT antibody was incubated with an excess of the immunogenic peptide before its incubation with the nitrocellulose strips. (B) Western blotting with the affinity-purified antibody against a peptide in the specific domain of βIV spectrin (βIV-SD) on 50 μg protein from rat brain PNS (brain, lanes 1, 3, and 4) and homogenates of human pancreatic islets (islets, lanes 2 and 5). (brain + alk. phos., lane 3) Rat brain PNS was treated with calf intestine alkaline phosphatase for 1 h at 37°C. (lanes 4 and 5) Western blotting with the βIV-SD antibody after preincubation with its antigenic peptide.