Active site ligand binding by an inactive ribonuclease S analogue. A quantitative affinity chromatographic study.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
1. The Preparation of Subtilisin-modified Ribonuclease and the Separation of the Peptide and Protein Components
2. Synthesis, Purification, and Properties of a Semisynthetic Ribonuclease S Incorporating 4-Fluoro-l-histidine at Position 12
3. Analysis of ribonuclease-nucleotide interactions by quantitative affinity chromatography.
4. Quantitative Affinity Chromatography. Determination of Binding Constants by Elution with Competitive Inhibitors
5. Evaluation of equilibrium constants by affinity chromatography
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1. Studies on polypeptides XXXIX. The role of the imidazole tele-nitrogen atom of histidine-12 in the catalytic action of RNase S′;Recueil des Travaux Chimiques des Pays-Bas;2010-09-02
2. An enantioselective synthesis of (S)-4-fluorohistidine;Journal of Fluorine Chemistry;2008-09
3. Recent developments in quantitative affinity chromatography;Journal of Chromatography A;1992-04
4. The study of ligand-protein interactions utilizing affinity chromatography;Applied Biochemistry and Biotechnology;1984-06
5. Structural Bases of Biological Function: From Nucleases to Neurophysins;The Impact of Protein Chemistry on the Biomedical Sciences;1984
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