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  • Title: Heat-stable translational inhibitor from rabbit reticulocyte lysates.
    Author: Gaitero F, Mendez E, de Haro C.
    Journal: FEBS Lett; 1989 Nov 06; 257(2):297-301. PubMed ID: 2583276.
    Abstract:
    We have purified to apparent homogeneity a heat-stable (HS) factor from the postribosomal supernatant of rabbit reticulocyte lysates [(1988) FEBS Lett. 236, 479-483]. HS inhibits translation in hemin-supplemented lysates and induces phosphorylation of the alpha-subunit of the eukaryotic initiation factor 2 as does hemin deficiency. The translational inhibition produced by addition of HS to hemin-containing reticulocyte lysates and the accompanying phosphorylation of the eIF-2 alpha subunit can be prevented or reversed by NADPH generators including glucose 6-phosphate, NADPH itself, and also by dithiols, e.g., dithiothreitol, but not by fructose 1,6-bisphosphate or by monothiols, e.g., 2-mercaptoethanol. When added to crude preparations of the proinhibitor form (proHCI) of the heme-controlled translational inhibitor (HCI), HS produces a pronounced increase of the HCI to proHCI ratio. It appeared possible that HS might be oxidized glutathione (GSSG) but this is not the case, for HS is not a substrate for highly purified glutathione reductase from rabbit erythrocytes. The spectral analysis of highly purified HS is consistent with the idea that HS could be a nucleotide derivative.
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