Use of antipeptide antibodies to probe the catalytic activity of p37v-mos.
Several site-directed antipeptide antibodies were generated to probe the kinase function of p37v-mos. Anti-mos(37-55) antibodies allowed autophosphorylation of p37v-mos, as well as transphosphorylation of exogenously added purified bovine vimentin. Rabbit antipeptide antibodies against v-mos residues 158-70, 194-206, 260-271, and 363-374 and a mouse monoclonal antibody against residues 344-359 completely inhibited p37v-mos protein kinase activity in vitro. p37v-mos autophosphorylation and vimentin transphosphorylation were affected similarly. These results suggest important roles for insert and the carboxy-terminal domains in the catalytic activity of p37v-mos.
Singh
B
B
University of Texas M.D. Anderson Cancer Center, Houston 77030.
al-Bagdadi
F
F
Liu
J X
JX
Arlinghaus
R B
RB
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002460:Cell Line; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D017232:Oncogene Proteins v-mos; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D015682:Retroviridae Proteins, Oncogenic / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D017232:Oncogene Proteins v-mos; D015682:Retroviridae Proteins, Oncogenic; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases