A rapid purification of synapsin I: A neuron specific spectrin binding protein

K. E. Krebs, I. S. Zagon, S. R. Goodman

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

We have developed a one Chromatographic step isolation protocol for the neuron specific protein synapsin I. This procedure results in a yield of 80 μg/g brain, which is ten fold better than the highest yield yet reported for this protein. The authenticity of the synapsin I isolated by this procedure is demonstrated by comigration with authentic synapsin I on SDS-polyacrylamide gels, crossreactivity with antibody specific against synapsin I, and nearly identical two dimensional chrymotryptic iodopeptide maps of authentic synapsin I and the protein purified by this protocol. Synapsin 1 isolated by this procedure retains its functional properties, demonstrated by the ability of synapsin I to stimulate the formation of a brain spectrin(240/235)/synapsin I/F-actin ternary complex as determined by a low shear falling ball viscometry assay. This novel protocol therefore has the advantage of being a rapid, high yield procedure that retains the functional properties of synapsin I.

Original languageEnglish (US)
Pages (from-to)237-241
Number of pages5
JournalBrain Research Bulletin
Volume17
Issue number2
DOIs
StatePublished - Aug 1986

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Synapsins
Neurons
Iodoproteins
spectrin-binding proteins
Spectrin
Proteins
Brain
Actins

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Cite this

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A rapid purification of synapsin I : A neuron specific spectrin binding protein. / Krebs, K. E.; Zagon, I. S.; Goodman, S. R.

In: Brain Research Bulletin, Vol. 17, No. 2, 08.1986, p. 237-241.

Research output: Contribution to journalArticle

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