protein synthesis in rabbit reticulocytes: a radioimmu noassay method for direct determination of eif-2 concen trations in reticulocyte lysates

نویسندگان

bahram. gh. yaghmai

naba.k.gupta

چکیده

a radioimmunoassay method for direct determination of eif-2 concentration in reticulocyte lysate has been developed. this assay method measures eif-2 concentratio ns in nanogram range. a value of 40 pmol eif-2 per ml of reticulocyte lysate was obtained.

Sign up for free to access the full text

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Protein synthesis in rabbit reticulocytes: characteristics of CO-eIF-2 protein complex.

A high molecular weight reticulocyte protein factor, named Co-eIF-2, contains Co-eIF-2A, Co-eIF-2B, and Co-eIF-2C activities and stimulates Met-tRNAf binding to eIF-2 both in the presence and absence of Mg2+. Some characteristics of this stimulation in the absence of Mg2+ are: (1) Stimulation is most pronounced at low eIF-2 levels. (2) Stimulation is partially resistant to heat and NEM treatmen...

متن کامل

Protein synthesis in rabbit reticulocytes: a study of the mechanism of action of the protein factor RF that reverses protein synthesis inhibition in heme-deficient reticulocyte lysates.

A eukaryotic initiation factor 2 (eIF-2)-ancillary protein factor Co-eIF-2 promotes displacement of GDP from eIF-2 X GDP and facilitates ternary complex (Met-tRNAf X eIF-2 X GTP) formation in the presence of Mg2+. Heme-regulated protein synthesis inhibitor, HRI, phosphorylates the alpha-subunit of eIF-2 and thus inhibits ternary complex formation as Co-eIF-2 does not displace GDP from eIF-2 alp...

متن کامل

Purification and characterization of protein synthesis initiation factors eIF-1, eIF-4C, eIF-4D, and eIF-5 from rabbit reticulocytes.

Protein synthesis initiation factors eIF-1, eIF-4C, eIF4D, and eIF-5 were isolated and purified from rabbit reticulocyte lysates. Crude initiation factors from the high salt ribosomal extract were separated by ammonium sulfate precipitation into Fraction A (0 to 40% saturation) and Fraction BC (40 to 70% saturation). Fraction BC was separated by gel filtration on Sephadex G-100 into two fractio...

متن کامل

Protein synthesis in rabbit reticulocytes: characteristics of the protein factor RF that reverses inhibition of protein synthesis in heme-deficient reticulocyte lysates.

During heme deficiency in reticulocyte lysates, the heme-regulated translational inhibitor of protein synthesis (HRI) is activated and shuts off protein synthesis. In partial reactions, HRI phosphorylates the Mr 38,000 subunit (alpha subunit) of eukaryotic initiation factor 2 (eIF-2), which forms a ternary complex, Met-tRNAf X eIF-2 X GTP. The eIF-2 alpha (P) thus formed is not recognized by tw...

متن کامل

Characterization of a rat liver factor that inhibits initiation of protein synthesis in rabbit reticulocyte lysates.

Protein synthesis in rabbit reticulocytes and their lysates is regulated by heme. In heme-deficient reticulocyte lysates, protein synthesis proceeds at the initial rate for several minutes and then declines abruptly. Inhibition of protein synthesis is due to the activation of a heme-regulated translational inhibitor (HRI) which blocks the initiation of protein synthesis. Addition of the isolate...

متن کامل

Protein synthesis in rabbit reticulocytes: characteristics of a ribosomal factor that reverses inhibition of protein synthesis in heme-deficient lysates.

A ribosomal salt (0.5 M KCl) wash factor (RF) that reverses inhibition of protein synthesis in heme-deficient reticulocyte lysates has been resolved from the bulk of Met-tRNAfMet-binding factor (EIF-1), Co-EIF-1, and EIF-2 (ternary complex dissociation factor, TDF). The purified RF restores protein synthesis activity of heme-deficient lysates to the level observed in the presence of hemin. No d...

متن کامل

منابع من

با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید


عنوان ژورنال:
acta medica iranica

جلد ۲۷، شماره ۱-۴، صفحات ۱-۱۳

کلمات کلیدی

میزبانی شده توسط پلتفرم ابری doprax.com

copyright © 2015-2023