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


Erdogdu G., Dholakia J., Wahba A.

ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, cilt.53, ss.897-901, 1998 (SCI İndekslerine Giren Dergi)

  • Cilt numarası: 53
  • Basım Tarihi: 1998
  • Dergi Adı: ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES
  • Sayfa Sayısı: ss.897-901

Özet

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.