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Purification of axonin-1, a protein that is secreted from axons during neurogenesis

Ruegg, M. A. and Stoeckli, E. T. and Kuhn, T. B. and Heller, M. and Zuellig, R. and Sonderegger, P.. (1989) Purification of axonin-1, a protein that is secreted from axons during neurogenesis. The EMBO Journal, 8 (1). pp. 55-63.

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Official URL: http://edoc.unibas.ch/dok/A5258440

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Abstract

Using selective metabolic labelling in a compartmental cell culture system two proteins, denoted axonin-1 and axonin-2, were found to be secreted by axons of dorsal root ganglia neurons from chicken embryos. Based on its characteristic coordinates and spot morphology in two-dimensional gel electrophoresis, axonin-1 was detected in the cerebrospinal fluid and the vitreous fluid, axonin-1 was purified 476-fold to homogeneity by a four-step chromatographic procedure. The identity of the purified protein as axonin-1 was confirmed by immunological methods. Axonin-1 is a glycoprotein that subdivides into at least 16 immunologically similar isoelectric variants; their molecular weight range extends from 132 to 140 kd and their pI range from 5.3 to 6.2. In the vitreous fluid of the embryo, axonin-1 could first be detected on the embryonic day 5 and highest concentrations were measured during the second half of embryonic life; in the vitreous fluid of the adult chicken, concentrations were approximately 20 times lower. The early onset of secretion and the time course of expression suggest a role for axonin-1 in the development of the nervous system.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Neurobiology > Pharmacology/Neurobiology (Rüegg)
UniBasel Contributors:Rüegg, Markus A.
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:0261-4189
e-ISSN:1460-2075
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:15 Nov 2017 14:10
Deposited On:22 Mar 2012 13:20

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