Studies on the Tryptophan Residues in Porcine Pepsin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Competitive Inhibition of Pepsin by Aliphatic Alcohols
2. Kinetics of the Pepsin-Catalyzed Hydrolysis of N-Acetyl Dipeptides*
3. Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution
4. A Highly Reactive Colored Reagent with Selectivity for the Tryptophan Residue in Proteins. 2-Hydroxy-5-nitrobenzyl Bromide1
5. A Colorimetric Procedure for the Quantitative Determination of Tryptophan Residues in Proteins
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1. INTERPRETATION AND APPLICATIONS OF THERMAL DIFFERENCE SPECTRA OF PROTEINS;International Journal of Peptide and Protein Research;2009-01-12
2. The Mechanism of the Catalytic Action of Pepsin and Related Acid Proteinases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry;Biochemical and Biophysical Research Communications;2003-12
4. Identification of tryptophanyl residues involved in binding of carbohydrate ligands to barley α-amylase 2;Carlsberg Research Communications;1987-11
5. Chapter 1 Aspartyl proteinases;Hydrolytic Enzymes;1987
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