Abstract
Several site-directed antipeptide antibodies were generated to probe the kinase function of p37v-mos. Anti-mos(3755) antibodies allowed autophosphorylation of p37v-mos, as well as transphosphorylation of exogenously added purified bovine vimentin. Rabbit antipeptide antibodies against v-mos residues 158-170, 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.
Original language | English (US) |
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Pages (from-to) | 535-542 |
Number of pages | 8 |
Journal | Virology |
Volume | 178 |
Issue number | 2 |
DOIs | |
State | Published - Oct 1990 |
ASJC Scopus subject areas
- Virology