| Autor: |
Tuck, Martin T., Cox, Ray |
| Zdroj: |
Carcinogenesis; 1982, Vol. 3 Issue 12, p1477-1480, 4p |
| Abstrakt: |
In a previous report, administration of [H]ethylethionine to partially hepatectomized rats was shown to ethylate two classes of proteins extracted from rat liver nuclei in 0.25 N HCI. Upon acid hydrolysis of the proteins, ethyl derivatives of both lysine and arginine were found. The arginine derivative which represented the major ethylated product is Identified in this report as N-monoethylarginine by the use of alkali hydrolysis. Administration of methionine along with the ethionine partially inhibited the ethylation. This suggests that the ethylation may proceed in a simlar manner to normal protein methylation by which the methylases utilize S-adenosylmethionine as the ethyl donor. Using assays for both protein-lysine and protein-arginine methyltransferase it was found that only the protein-arginine methyltransferase could use radiolabeled S-adenosylmethionine as a substrate. The major product formed in this assay was identified as N-monoethylarginine. [ABSTRACT FROM PUBLISHER] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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