科研之友
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摘要
Polyclonal antisera were generated against synthetic peptides corresponding to distinct regions of the rap1 protein sequences. A "rap1-common" antiserum, prepared against an 18-amino acid segment of the rap1a protein near the proposed GTP-binding region, reacted with both rap1a and rap1b recombinant proteins expressed in Escherichia coli and with two low molecular weight GTP-binding proteins of 22 and 24 kDa in unstimulated human platelets. An antiserum raised against a carboxyl-terminal peptide of rap1b containing the putative site of post-translational processing reacted strongly with bacterial-expressed recombinant rap1b and with a 24-kDa GTP-binding protein in platelets, but not with recombinant rap1a or a 22-kDa GTP-binding protein. The mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of this rap1b immunoreactive protein coincided with that of bacterial-expressed rap1b and not with the faster migrating form of rap1b that incorporates radioactivity from [H-3]mevalonic acid in the insect/baculovirus system. This suggests that our rap1b-specific antiserum recognizes only one form of rap1b, that which has not undergone carboxyl-terminal post-translational processing.
- 出版日期1991-3-5
