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Purification and some properties of an oxydative inhibitor in rabbit reticulocyte lysates
Date
1998-09-01
Author
Erdogdu, G
Dholakia, JN
Wahba, AJ
Metadata
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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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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 alh 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 mu g), protein synthesis in the inhibited reticulocyte lysate will be already recovered.
Subject Keywords
Phosphorylation
,
Cells
,
Physiological stresses
,
Heat-shock
,
Protein-synthesis initiation
,
Regulated eif-2-alpha kinase
,
Stable translational inhibitor
,
Initiation factor-ii
,
Nucleotide-exchange factor
URI
https://hdl.handle.net/11511/66238
Journal
ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES
Collections
Technical Vocational School of Higher Education, Article
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G. Erdogdu, J. Dholakia, and A. Wahba, “Purification and some properties of an oxydative inhibitor in rabbit reticulocyte lysates,”
ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES
, pp. 897–901, 1998, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/66238.