Reinvestigation of the phenacyl bromide modification of α-chymotrypsin
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00662a018
Reference24 articles.
1. Inactivation of α-chymotrypsin by a bifunctional reagent, 2-bromomethyl-3,1-benzoxazin-4-one
2. The formation and activities of substituted phenacylchymotrypsins
3. The photofragmentation and photoaffinity labeling of phenacyl and naphthacyl α-chymotrypsins
4. Evidence for Conformational Changes in α-Chymotrypsin Catalyzed Reactions. VII. Thermal Induced Reversible Changes of Conformation at pH 2.0
5. Environment of a reporter group at the active site of chymotrypsin
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1. Reduction−Oxidation Control of β-Sheet Assembly in Genetically Engineered Silk;Biomacromolecules;2000-10-04
2. Designing recombinant spider silk proteins to control assembly;International Journal of Biological Macromolecules;1999-03
3. Reactivity of bromide for radiolabeling of proteins and peptides;Applied Radiation and Isotopes;1997-07
4. α-Bromo-4-amino-3-nitroacetophenone, a new reagent for protein modification. Modification of the methionine-290 residue of porcine pepsin;Biochemical Journal;1980-05-01
5. Hepatic microsomal epoxide hydrase. Involvement of a histidine at the active site suggests a nucleophilic mechanism.;Journal of Biological Chemistry;1978-05
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