L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I
作者： M E Huflejt , C W Turck , R Lindstedt , S H Barondes , H Leffler
DOI: 10.1016/S0021-9258(19)74371-3
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摘要: 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) Biol. Chem. 265, 17706-17712), which contain small amount of this protein. We have determined the site phosphorylation on taking advantage abundance L-29 (about 1% total cell protein) polarized Madin-Darby canine kidney (MDCK) cells. Approximately 15-20% is these Phosphoamino acid analysis showed phosphate incorporation only at serine. Analysis chymotryptic endoproteinase Asp-N-generated NH2-terminal fragments by Edman degradation that 90% Ser6 10% Ser12. The sequence surrounding Ser6, conserved all known sequences, indicated serine might casein kinase I or II. Reaction human recombinant with [gamma-32P]ATP each kinases catalyzed significant 32P into L-29; and, as from MDCK extracts, most incorporated
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