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Updated: Sep 21, 2026

Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
Interaction of puromycin with acceptor site of human placenta 80 S ribosomes
D M Graifer1, O S Fedorova, G G Karpova
1Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, Novosibirsk.
Abstract:
The complex N-AcPhe-tRNA(Phe).poly(U).80 S ribosome from human placenta was treated with puromycin taken in various concentrations. Based on the kinetic data of N-acetylphenylalanyl-puromycin formation, the association constant of puromycin with the acceptor site of the ribosome was estimated to be (3.96 +/- 0.84) x 10(4) M-1 at 37 degrees C.
Insights
This study investigated puromycin binding to human placental ribosomes. The association constant for puromycin at the ribosome acceptor site was determined to be approximately 4 x 10^4 M^-1.
Area of Science:
- Molecular Biology
- Biochemistry
- Human Placenta Research
Background:
- Ribosomes are essential for protein synthesis.
- Puromycin is an antibiotic that inhibits translation.
- Understanding drug-ribosome interactions is crucial for developing new therapeutics.
Purpose of the Study:
- To determine the binding affinity of puromycin to the human placental 80S ribosome.
- To investigate the kinetics of N-acetylphenylalanyl-puromycin formation.
Main Methods:
- Treatment of human placental 80S ribosomes with N-AcPhe-tRNA(Phe) and poly(U).
- Incubation with varying concentrations of puromycin.
- Kinetic analysis of N-acetylphenylalanyl-puromycin formation.
Main Results:
- The association constant of puromycin with the ribosome acceptor site was estimated.
- The calculated association constant was (3.96 +/- 0.84) x 10^4 M^-1 at 37°C.
Conclusions:
- Puromycin exhibits a moderate binding affinity to the human placental ribosome acceptor site.
- This quantitative data provides insights into the mechanism of translation inhibition by puromycin.
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