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Rapid Production of Recombinant Human SLFN14 Ribonuclease and Stoichiometric Analysis by Mass Photometry
Published on: February 20, 2026
CRYSTALLINE RIBONUCLEASE
1Laboratories of The Rockefeller Institute for Medical Research, Princeton, New Jersey.
The Journal of General Physiology
|October 30, 2009
Summary
Researchers isolated a crystalline enzyme, ribonuclease, from beef pancreas that digests yeast nucleic acid. This enzyme breaks down nucleic acid into smaller fragments, aiding in biochemical research.
Area of Science:
- Biochemistry
- Molecular Biology
Background:
- Enzymes play crucial roles in biological processes.
- Nucleic acids are fundamental molecules of life.
Purpose of the Study:
- To isolate and characterize a novel enzyme capable of digesting yeast nucleic acid.
- To understand the properties and activity of this enzyme.
Main Methods:
- Crystallization of the enzyme from beef pancreas.
- Characterization of the enzyme's physical and chemical properties (molecular weight, isoelectric point).
- Analysis of the enzyme's effect on yeast nucleic acid digestion and product analysis.
Main Results:
- A crystalline enzyme, ribonuclease, was isolated from beef pancreas.
- Ribonuclease is a soluble albumin-type protein with a molecular weight of approximately 15,000 and an isoelectric point around pH 8.0.
- The enzyme effectively digests yeast nucleic acid into smaller, non-precipitable fragments, with acid group formation but minimal phosphoric acid liberation.
- Ribonuclease exhibits stability over a wide pH range, with optimal stability between pH 2.0 and 4.5, and its activity is sensitive to denaturation.
Conclusions:
- Ribonuclease is a stable enzyme with specific activity against yeast nucleic acid.
- The enzyme's properties suggest its utility in biochemical research for nucleic acid analysis.
- Enzymatic activity is directly linked to the structural integrity of the ribonuclease protein.
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