Molecular characterization of an ependymin precursor from goldfish brain.

Abstract:

:Ependymins are thought to be implicated in fundamental processes involved in plasticity of the goldfish CNS. Gas-phase sequencing of purified ependymins beta and gamma revealed that they share the same N-terminal sequence. Each sequence displays microheterogeneities at several positions. Based on the protein sequences obtained, we constructed synthetic oligonucleotides and used them as hybridization probes for screening cDNA libraries of goldfish brain. In this article we describe the full-length sequence of a mRNA encoding a precursor of ependymins. A cleavable signal sequence characteristic of secretory proteins is located at the N-terminal end, followed directly by the ependymin sequence. Also, two potential N-glycosylation sites were detected. A computer search revealed that ependymins form a novel family of unique proteins.

journal_name

J Neurochem

authors

Königstorfer A,Sterrer S,Eckerskorn C,Lottspeich F,Schmidt R,Hoffmann W

doi

10.1111/j.1471-4159.1989.tb10932.x

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

310-2

issue

1

eissn

0022-3042

issn

1471-4159

journal_volume

52

pub_type

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