| Autor: |
L Chu, Carol-Ann Ohmstede, Bryan R. Reep, Eduardo G. Lapetina, Deborah A. Winegar |
| Rok vydání: |
1991 |
| Předmět: |
|
| Zdroj: |
Journal of Biological Chemistry. 266:4375-4380 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(20)64332-0 |
| Popis: |
Polyclonal antisera were generated against synthetic peptides corresponding to distinct regions of the rap 1 protein sequences. A "rap 1-common" antiserum, prepared against an 18-amino acid segment of the rap 1a protein near the proposed GTP-binding region, reacted with both rap 1a and rap 1b 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 rap 1b containing the putative site of post-translational processing reacted strongly with bacterial-expressed recombinant rap 1b and with a 24-kDa GTP-binding protein in platelets, but not with recombinant rap 1a or a 22-kDa GTP-binding protein. The mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of this rap 1b immunoreactive protein coincided with that of bacterial-expressed rap 1b and not with the faster migrating form of rap 1b that incorporates radioactivity from [3H]mevalonic acid in the insect/baculovirus system. This suggests that our rap 1b-specific antiserum recognizes only one form of rap 1b, that which has not undergone carboxyl-terminal post-translational processing. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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