Autor: |
Kudlicki W; Department of Chemistry and Biochemistry, University of Texas, Austin 78712., Picking WD, Kramer G, Hardesty B, Smailov SK, Mukhamedzhanov BG, Lee AV, Iskakov BK |
Jazyk: |
angličtina |
Zdroj: |
European journal of biochemistry [Eur J Biochem] 1991 May 08; Vol. 197 (3), pp. 623-9. |
DOI: |
10.1111/j.1432-1033.1991.tb15952.x |
Abstrakt: |
Polyproanthocyanidin (PPA), a phenolic polymer isolated from the plant Alhagi kirgisorum S. was found to interact strongly with eukaryotic initiation factor 2 (eIF-2), thereby inhibiting reactions involving this protein. When added to a rabbit reticulocyte lysate system, PPA blocks in vitro translation and it appears to selectively bind and precipitate a relatively small number of proteins including eIF-2 and regulin. The phosphorylation of purified regulin and eIF-2 by casein kinase II (CK II) and the heme-sensitive eIF-2 alpha kinase, respectively, was also inhibited by the polyphenolic compound. The natural fluorescence of PPA was utilized to compare its interaction with eIF-2 and regulin to that with other natural and synthetic polypeptides. |
Databáze: |
MEDLINE |
Externí odkaz: |
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