Degradation of glial fibrillary acidic protein by a calcium dependent proteinase: an electroblot study.

@article{DeArmond1983DegradationOG,
  title={Degradation of glial fibrillary acidic protein by a calcium dependent proteinase: an electroblot study.},
  author={Stephen J. DeArmond and Marta Fajardo and S A Naughton and L. F. Eng},
  journal={Brain research},
  year={1983},
  volume={262 2},
  pages={275-82}
}
In situ and in vitro degradation of glial fibrillary acidic (GFA) protein in mouse spinal cord was examined with electroblots stained for GFA protein by the peroxidase anti-peroxidase method. Non-degraded, intact GFA protein had a molecular weight of 48 Kdaltons and isoelectric points ranging from pH 5.8 to 6.4. The molecular weights of immunoreactive degradation products ranged from 47 to 28 Kdaltons. All of the degradation products had acid shifted isoelectric points (pH 5.8-5.2). Degradation… CONTINUE READING

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