Purification and some properties of an oxydative inhibitor in rabbit reticulocyte lysates

Date

1998-09-01

Author

Erdogdu, G
Dholakia, JN
Wahba, AJ

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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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Citation Formats

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.