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)


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).


Protein Sequence Data Dent Protein Kinase Endogenous Protein Kinase Retinal Cell Neuron Purify Protein Kinase 
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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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