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. 2000 Nov 27;151(5):1013–1024. doi: 10.1083/jcb.151.5.1013

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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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SMI31 and RT97 are distinct NFH phosphoepitopes. (A) NFH peptides after chymotryptic digestion were separated by HPLC, and aliquots of all fractions were immunostained in slot blots with SMI34, SMI31, or RT97. Fractions containing high SMI34 or SMI31 signal and no RT97 signal are indicated by arrowheads. (B) NFH tryptic digest peptides after tryptic digestion were affinity purified with either RT97 or SMI31 antibodies. The slot blots of eluted fractions from SMI31 and RT97 affinity columns probed with RT97 antibody (top panel) or with SMI31 antibody (bottom panel). (C) Two-dimensional PAGE immunoblots of NFH from adult optic nerve cytoskeletal fractions probed with SMI33 to detect total NFH or the RT97 phosphoepitope. All blots were also immunostained with an antibody against NFL used as an internal standard to confirm the pH range. RT97 recognizes only the most acidic (highly phosphorylated) NFH isoforms (pH 5.9 to 5.1). IEF, Isoelectric focusing.