L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I.

@article{Huflejt1993L29AS,
  title={L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I.},
  author={Margaret E. Huflejt and Christoph Wilhelm Turck and Ragnar Lindstedt and S H Barondes and Hakon Leffler},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 35},
  pages={26712-8}
}
L-29, a mammalian soluble lactose-binding lectin, was previously shown to be phosphorylated in confluent 3T3 fibroblasts (Cowles, E. A., Agrwal, N., Anderson, R. L., and Wang, J. L. (1990) J. Biol. Chem. 265, 17706-17712), which contain a small amount of this protein. We have determined the site of phosphorylation on L-29, taking advantage of the abundance of L-29 (about 1% of total soluble cell protein) in confluent polarized Madin-Darby canine kidney (MDCK) cells. Approximately 15-20% of the… CONTINUE READING

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