Modulation of the catalytic properties of α-chymotrypsin by chemical modification at Tyr 146
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference26 articles.
1. Selective chemical modification of proteins.
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3. A Change in Specificity of Chymotrypsin Caused by Chemical Modification of Methionine Residues
4. The Catalytic Activity of Methionine-S-(N-2-carboxyisopropyl)carbamylmethylsulfonium Bromide-192-α-chymotrypsin
5. Allosteric Activation of the Hydrolysis of Specific Substrates by Chymotrypsin
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1. Modification of Hydroxyl and Carboxyl Functional Groups in Proteins;Chemical Modification of Biological Polymers;2011-09-13
2. Quantification of azo-coupled lysine in azo proteins by amino acid analysis;Analytical Biochemistry;1986-08
3. Preparation and characterization of sulfanilazo and arsanilazo proteins;Biochemistry;1984-02-14
4. Quantitative affinity chromatography of α-chymotrypsin;Archives of Biochemistry and Biophysics;1979-12
5. Development of a method for the incorporation of substitution-inert metal ions into proteins. Site-specific modification of arsanilazotyrosine-248 carboxypeptidase A with cobalt(III);Biochemistry;1979-10-01
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