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Neurochemical Research

, Volume 19, Issue 2, pp 223–227 | Cite as

Structure-function studies of human ciliary neurotrophic factor

  • Alessandro Negro
  • Vincenza Corsa
  • Giuseppe Corona
  • Claudio Grandi
  • Stephen D. Skaper
  • Lanfranco Callegaro
Original Articles

Abstract

Ciliary neurotrophic factor (CNTF) is a polypeptide that promotes the survival and/or differentiation of a number of neural cell types. Here we present a structural and functional analysis of the human CNTF molecule. Variant proteins were synthesized byEscherichia coli trnsformmed with mutant cDNA constructs, and purified by SDS-polyacrylamide gel electrophoresis and reverse phase high pressure liquid chromatography. Most variant CNTF proteins lacked neurotrophic activity, but two N-and C-terminal deletions (Δ2–14 and Δ173–200, respectively) actually displayed a several-fold increase in specific activity. Loss of biological activity was accompanied by changes in the alphahelical nature of CNTF as measured by circular dichroism. These data strengthen the proposed similarity between CNTF and the family of hematopoietic cytokines.

Key Words

Ciliary neurotrophic factor mutagenesis secondeary protein structure biological activity 

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Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Alessandro Negro
    • 1
  • Vincenza Corsa
    • 2
  • Giuseppe Corona
    • 1
  • Claudio Grandi
    • 3
  • Stephen D. Skaper
    • 1
  • Lanfranco Callegaro
    • 2
  1. 1.Fidia Research LaboratoriesFIDIA S.p.A.Abano TermeItaly
  2. 2.Fidia Advanced BiopolymersFIDIA S.p.A.Abano TermeItaly
  3. 3.Dept. of Organic ChemistryUniversity of PaduaItaly

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