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A rat brain protein kinase phosphorylating specifically neurofilaments
Author(s) -
Toru-Delbauffe D.,
Pierre M.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80761-3
Subject(s) - neurofilament , phosphorylation , protein kinase a , biochemistry , kinase , chemistry , sucrose gradient , casein kinase 2 , ultracentrifuge , histone , casein kinase 2, alpha 1 , casein kinase 1 , protein subunit , casein , microbiology and biotechnology , mitogen activated protein kinase kinase , biology , enzyme , immunohistochemistry , dna , immunology , gene
Protein kinase activities associated with neurofilament (cAMP, cGMP, Ca 2+ ‐independent) were almost completely extracted by 0.8 M KCl. Two activities were separated by either sucrose gradient ultracentrifugation of phosphocellulose chromatography. One of them phosphorylates specifically neurofilament proteins and preferentially the triplet (200 kDA, 145 kDa and 68 kDa) but neither casein nor type II A histone. The second activity was identified as casein kinase I and does not catalyze the phosphorylation of neurofilament protein.