p56lck stably associates with a 115 kDa substrate.
Using antibodies directed against p56lck, we have identified a 115 kDa protein (p115) that is specifically immunoprecipitated with p56lck from whole cell lysates. The p56lck/p115 complex is stable in the presence of nonionic detergents. p115 becomes phosphorylated on tyrosine residues in p56lck immune-complex kinase assays. Treatment of whole cells with 12-O-tetradecanoyl phorbol-13-acetate decreases the subsequent tyrosine phosphorylation of p115 in immune-complex kinase assays.
Srinivas
P R
PR
Department of Medicinal Chemistry and Pharmacognosy, Purdue University, West Lafayette, IN 47907.
Hutchcroft
J E
JE
Aube
B D
BD
Harrison
M L
ML
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000936:Antigen-Antibody Complex; D002460:Cell Line; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D051379:Mice; D008970:Molecular Weight; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000302:isolation & purification / Q000378:metabolism*; D013601:T-Lymphocytes / Q000201:enzymology / Q000276:immunology*
D000936:Antigen-Antibody Complex; D003902:Detergents; D009856:Oncogene Proteins, Viral; D000255:Adenosine Triphosphate; D011505:Protein-Tyrosine Kinases; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck)