The Identification of a Tryptophan Residue Essential to the Catalytic Activity of Bovine Pancreatic Deoxyribonuclease
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. The Reactivity toward N-Bromosuccinimide of Tryptophan in Enzymes, Zymogens, and Inhibited Enzymes*
2. SELECTIVE CLEAVAGE OF PEPTIDE BONDS. II. THE TRYPTOPHYL PEPTIDE BOND AND THE CLEAVAGE OF GLUCAGON1
3. Chemical Cleavage of Proteins
4. The action of N-bromosuccinimide on chymotrypsin
5. A Colorimetric Procedure for the Quantitative Determination of Tryptophan Residues in Proteins
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1. MOLAR ABSORPTIVITY AND A1%1cm VALUES FOR PROTEINS AT SELECTED WAVELENGTHS OF THE ULTRAVIOLET AND VISIBLE REGION. V*;International Journal of Peptide and Protein Research;2009-01-12
2. Purification and properties of ribonuclelase E, an RNA-processing enzyme from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1983-09
3. Reactivity of the tryptophan residues in bovine pancreatic deoxyribonuclease with N-bromosuccinimide.;Journal of Biological Chemistry;1980-09
4. A method for measuring the number of single- and double-strand breaks introduced into DNA molecules by the action of deoxyribonucleases;Analytical Biochemistry;1978-10
5. Characterization of an endoribonuclease, RNase N, from Escherichia coli;Journal of Biological Chemistry;1978-08
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