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Phosphorylation protects neurofilaments against proteolysis
- Source :
- Journal of Neuroimmunology. 14:149-160
- Publication Year :
- 1987
- Publisher :
- Elsevier BV, 1987.
-
Abstract
- During incubation with phosphatase, the 200 kDa neurofilament protein in cytoskeletal preparations is degraded extensively. Degradation, which is divalent cation-independent, does not occur when inhibitors of phosphatase are added. The 160 kDa chymotryptic fragment of neurofilaments or affinity-purified 200 kDa protein are not degraded by phosphatase. The results suggest that (1) phosphorylated neurofilaments are protected against proteolysis, and (2) dephosphorylated neurofilaments are degraded by a calcium-independent, endogenous proteinase which is associated with assembled neurofilaments or with other cytoskeletal components, and not with the phosphatase used.
- Subjects :
- Paper
Neurofilament
Proteolysis
Immunology
Immunocytochemistry
Phosphatase
Endogeny
Biology
Chromatography, Affinity
Divalent
Drug Stability
Intermediate Filament Proteins
Neurofilament Proteins
medicine
Chymotrypsin
Immunology and Allergy
Phosphorylation
Cytoskeleton
chemistry.chemical_classification
medicine.diagnostic_test
Collodion
Phosphoric Monoester Hydrolases
Neurology
Biochemistry
chemistry
Electrophoresis, Polyacrylamide Gel
Neurology (clinical)
Subjects
Details
- ISSN :
- 01655728
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Journal of Neuroimmunology
- Accession number :
- edsair.doi.dedup.....70370dbb2365596c059d9d27b8cd72a7