TY - JOUR
T1 - Identification of a New in Vitro Substrate of Tyrosine Protein Kinase
AU - Tokuda, Masaaki
AU - Kong, Siow Kee
AU - Khanna, Navin C.
AU - Waisman, David Morton
PY - 1987
Y1 - 1987
N2 - Recent studies in our laboratory [Tokuda, M., Khanna, N. C., Aurora, A., & Waisman, D. M. (1986) Biochem. Biophys. Res. Commun. 139, 910–917] have identified in membranes of rat spleen two tyrosine protein kinases named TPK-I and TPK-II. In this paper the identification of the Ca2+ binding protein CAB-48 as a major in vitro substrate of TPK-II is reported. TPK-II catalyzed the incorporation of 0.73 mol of phosphate/mol of CAB-48. Phosphoamino acid analysis revealed that phosphorylation of CAB-48 was specific for tyrosine residues. Phosphorylation of CAB-48 by TPK-I (rat spleen), protein kinase C, casein kinase I, casein kinase II, cAMP-dependent protein kinase, or calcium calmodulin dependent protein kinase was not observed.
AB - Recent studies in our laboratory [Tokuda, M., Khanna, N. C., Aurora, A., & Waisman, D. M. (1986) Biochem. Biophys. Res. Commun. 139, 910–917] have identified in membranes of rat spleen two tyrosine protein kinases named TPK-I and TPK-II. In this paper the identification of the Ca2+ binding protein CAB-48 as a major in vitro substrate of TPK-II is reported. TPK-II catalyzed the incorporation of 0.73 mol of phosphate/mol of CAB-48. Phosphoamino acid analysis revealed that phosphorylation of CAB-48 was specific for tyrosine residues. Phosphorylation of CAB-48 by TPK-I (rat spleen), protein kinase C, casein kinase I, casein kinase II, cAMP-dependent protein kinase, or calcium calmodulin dependent protein kinase was not observed.
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U2 - 10.1021/bi00391a002
DO - 10.1021/bi00391a002
M3 - Article
C2 - 3676248
AN - SCOPUS:0023664840
SN - 0006-2960
VL - 26
SP - 5226
EP - 5229
JO - Biochemistry
JF - Biochemistry
IS - 17
ER -