Dinitrophenylation of a single cysteine side chain in phosphorylasebfrom rabbit muscle with concomitant blocking of AMP binding
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(73)80065-1/fullpdf
Reference17 articles.
1. Active site peptides from glycogen phosphorylase
2. Dinitrophenylation of glycogen phosphorylase. I. Preparation and properties of active dinitrophenyl derivatives
3. Peptide sequences and relative reactivity of the reactive sulfhydryl groups of rabbit muscle phosphorylase
4. Relationship between Conformationally Sensitive Probe Binding Sites on Phosphorylase b
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1. Characterization of an ATPase on the Inside of Rat-Liver Nuclear Envelopes by Affinity Labeling;European Journal of Biochemistry;1982-10
2. Reversed-phase ion-pair chromatography with UV-absorbing ions in the mobile phase;Journal of Chromatography A;1981-11
3. Spin-labelling of phosphorylase b using a paramagnetic 1-fluoro-2,4-dinitrobenzene derivative;Biochimica et Biophysica Acta (BBA) - Protein Structure;1980-01
4. Crystallographic analysis at low resolution of metabolite binding sites on phosphorylase b;Journal of Molecular Biology;1978-02
5. Chemical Modification and Cleavage of Proteins and Chemical Strategy in Immunochemical Studies of Proteins;Immunochemistry of Proteins;1977
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