Abstract
We have observed the phosphorylation of neurofilament protein from squid axoplasm. Phosphorylation is demonstrated by 32P labeling of protein during incubation of axoplasm with [gamma-32P]ATP. When the labeled proteins are separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), two bands, at 2.0 x 10(5) daltons and greater than 4 x 10(5) daltons, contain the bulk of the 32P. The 2.0 x 10(5)-dalton phosphorylated polypeptide comigrates on SDS-PAGE with one of the subunits of squid neurofilament protein. Both major phosphorylated polypeptides co-fractionate with neurofilaments in discontinuous sucrose gradient centrifugation and on gel filtration chromatography on Sepharose 4B. The protein-phosphate bond behaves like a phospho-ester, and labeled phospho-serine is identified in an acid hydrolysate of the protein. The generality of this phenomenon in various species and its possible physiological significance are discussed.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 7:04 p.m.) |
Deposited | 2 years ago (July 24, 2023, 4:32 a.m.) |
Indexed | 1 month, 2 weeks ago (July 7, 2025, 2:02 a.m.) |
Issued | 47 years ago (Aug. 1, 1978) |
Published | 47 years ago (Aug. 1, 1978) |
Published Online | 47 years ago (Aug. 1, 1978) |
Published Print | 47 years ago (Aug. 1, 1978) |
@article{Pant_1978, title={Neurofilament protein is phosphorylated in the squid giant axon.}, volume={78}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.78.2.r23}, DOI={10.1083/jcb.78.2.r23}, number={2}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Pant, H C and Shecket, G and Gainer, H and Lasek, R J}, year={1978}, month=aug, pages={R23} }