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Evidence for Site- and Domain-Specific Phosphorylation of the 145-kDa Neurofilament Subunit InVivo

  • Ram K. Sihag
  • Ralph A. Nixon
Conference paper
Part of the NATO ASI Series book series (volume 56)

Abstract

A comparison of two-dimensional phosphopeptide maps of NF-M phosphorylated in vivo and in vitro in combination with protein sequence data showed that phosphate groups on the amino terminal head domain are added by protein kinase A and protein kinase C. By contrast, the phosphate groups on the carboxy-terminal domain, which account for about 90% of the phosphate on NF-M, are added by heparin-sensitive second-messenger-independent protein kinase(s).

Keywords

Protein Sequence Data Dent Protein Kinase Endogenous Protein Kinase Retinal Cell Neuron Purify Protein Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Ram K. Sihag
    • 1
  • Ralph A. Nixon
    • 1
  1. 1.Ralph Lowell Laboratories McLean HospitalHarvard Medical SchoolBelmontUSA

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