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Neurofilament protein is phosphorylated in the squid giant axon

We have observed the phosphorylation of neurofilament protein from squid axoplasm. Phosphorylation is demonstrated by 32P labeling of protein during incubation of axoplasm with [gamma-32P]ATP. When the labeled proteins are separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two bands, at...

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Detalles Bibliográficos
Autores principales: Pant, H. C., Shecket, G., Gainer, H., Lasek, R. J.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1978
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110134/
https://www.ncbi.nlm.nih.gov/pubmed/690167
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author Pant, H. C.
Shecket, G.
Gainer, H.
Lasek, R. J.
author_facet Pant, H. C.
Shecket, G.
Gainer, H.
Lasek, R. J.
author_sort Pant, H. C.
collection PubMed
description We have observed the phosphorylation of neurofilament protein from squid axoplasm. Phosphorylation is demonstrated by 32P labeling of protein during incubation of axoplasm with [gamma-32P]ATP. When the labeled proteins are separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two bands, at 2.0 x 10(5) daltons and greater than 4 x 10(5) daltons, contain the bulk of the 32P. The 2.0 x 10(5)-dalton phosphorylated polypeptide comigrates on SDS-PAGE with one of the subunits of squid neurofilament protein. Both major phosphorylated polypeptides co-fractionate with neurofilaments in discontinuous sucrose gradient centrifugation and on gel filtration chromatography on Sepharose 4B. The protein-phosphate bond behaves like a phospho-ester, and labeled phospho-serine is identified in an acid hydrolysate of the protein. The generality of this phenomenon in various species and its possible physiological significance are discussed.
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spelling pubmed-21101342008-05-01 Neurofilament protein is phosphorylated in the squid giant axon Pant, H. C. Shecket, G. Gainer, H. Lasek, R. J. J Cell Biol Rapid Communication We have observed the phosphorylation of neurofilament protein from squid axoplasm. Phosphorylation is demonstrated by 32P labeling of protein during incubation of axoplasm with [gamma-32P]ATP. When the labeled proteins are separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two bands, at 2.0 x 10(5) daltons and greater than 4 x 10(5) daltons, contain the bulk of the 32P. The 2.0 x 10(5)-dalton phosphorylated polypeptide comigrates on SDS-PAGE with one of the subunits of squid neurofilament protein. Both major phosphorylated polypeptides co-fractionate with neurofilaments in discontinuous sucrose gradient centrifugation and on gel filtration chromatography on Sepharose 4B. The protein-phosphate bond behaves like a phospho-ester, and labeled phospho-serine is identified in an acid hydrolysate of the protein. The generality of this phenomenon in various species and its possible physiological significance are discussed. The Rockefeller University Press 1978-08-01 /pmc/articles/PMC2110134/ /pubmed/690167 Text en 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/).
spellingShingle Rapid Communication
Pant, H. C.
Shecket, G.
Gainer, H.
Lasek, R. J.
Neurofilament protein is phosphorylated in the squid giant axon
title Neurofilament protein is phosphorylated in the squid giant axon
title_full Neurofilament protein is phosphorylated in the squid giant axon
title_fullStr Neurofilament protein is phosphorylated in the squid giant axon
title_full_unstemmed Neurofilament protein is phosphorylated in the squid giant axon
title_short Neurofilament protein is phosphorylated in the squid giant axon
title_sort neurofilament protein is phosphorylated in the squid giant axon
topic Rapid Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110134/
https://www.ncbi.nlm.nih.gov/pubmed/690167
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