TY - JOUR
T1 - Phosphorylation of fibrinogen by casein kinase 1
AU - Itarte, E.
AU - Plana, M.
AU - Guasch, M. D.
AU - Martos, C.
PY - 1983/12/16
Y1 - 1983/12/16
N2 - Casein kinase 1 phosphorylated human fibrinogen, in a reaction that did not use GTP as phosphoryl donor and was neither stimulated by cyclic AMP or Ca2+, nor inhibited by the cyclic AMP-dependent protein kinase inhibitor protein. Maximal incorporation averaged 4 mol of phosphate per mol of fibrinogen, most of it in the largest CNBr-fragment of the α-chain. Phosphoamino acid analysis revealed that phosphorylation occurred only at seryl residues. The phosphorylation of fibrinogen by casein kinase 1 was reverted by alkaline phosphatase. © 1983.
AB - Casein kinase 1 phosphorylated human fibrinogen, in a reaction that did not use GTP as phosphoryl donor and was neither stimulated by cyclic AMP or Ca2+, nor inhibited by the cyclic AMP-dependent protein kinase inhibitor protein. Maximal incorporation averaged 4 mol of phosphate per mol of fibrinogen, most of it in the largest CNBr-fragment of the α-chain. Phosphoamino acid analysis revealed that phosphorylation occurred only at seryl residues. The phosphorylation of fibrinogen by casein kinase 1 was reverted by alkaline phosphatase. © 1983.
U2 - https://doi.org/10.1016/0006-291X(83)91247-0
DO - https://doi.org/10.1016/0006-291X(83)91247-0
M3 - Article
SN - 0006-291X
VL - 117
SP - 631
EP - 636
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
ER -