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  • Title: Purification and some properties of an oxydative inhibitor in rabbit reticulocyte lysates.
    Author: Erdogdu G, Dholakia JN, Wahba AJ.
    Journal: Z Naturforsch C J Biosci; 1998; 53(9-10):897-901. PubMed ID: 9825544.
    Abstract:
    Protein synthesis in rabbit reticulocyte lysates in the presence of heme is inhibited by 50% by the addition of 4 mM GSSG (oxidized glutathione). The incubation of the rabbit reticulocyte lysate with 4 mM GSSG at 30 degrees C for 30 min will cause activation of an inhibitor of protein synthesis which could be purified from the lysates through a five-step procedure. The inhibitor results in a 70-80% inhibition after a 1 h incubation. The inhibitor consists of one polypeptide of 23 kDa apparent molecular weight and is 90% pure as judged by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. However, in the presence of cAMP (10 mM) or GEF (guanine nucleotide exchange factor) (0.3 microgram), protein synthesis in the inhibited reticulocyte lysate will be already recovered.
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