The effects of N-acetyltryptophan and caprylic acid on protein aggregation
Author:
Affiliation:
1. Institute of Applied Physics, University of Tsukuba
2. Alliance Protein Laboratories
Publisher
Japan Science Society of Biological Macromolecules
Subject
Molecular Biology
Link
https://www.jstage.jst.go.jp/article/jbm/16/1/16_3/_pdf
Reference13 articles.
1. [1] G. A. Ballou, P. D. Boyer, J. M. Luck, and F. G. Lum. (1944) The heat coagulation of human serum albumin. J. Biol. Chem., 153, 589–605.
2. [2] P. D. Boyer, F. G. Lum, G. A. Ballou, J. M. Luck, and R. G. Rice. (1946) The combination of fatty acids and related compounds with serum albumin I. stabilization against heat denaturation. J. Biol. Chem., 162, 181–198
3. [3] T. Arakawa and Y. Kita. (2000) Stabilizing effects of caprylate and acetyltryptophanate on heatinduced aggregation of bovine serum albumin. Biochim. Biophys. Acta BBA - Protein Struct. Mol. Enzymol., 1479, 32–36.
4. [4] J. L. Beare-Rogers, A. Dieffenbacher, and J. V. Holm. (2009) Lexicon of lipid nutrition (IUPAC technical report). Pure Appl. Chem., 73, 685–744.
5. [5] M. Anraku, Y. Tsurusaki, H. Watanabe, T. Maruyama, U. Kragh-Hansen, and M. Otagiri. (2004) Stabilizing mechanisms in commercial albumin preparations: octanoate and N-acetyl-ltryptophanate protect human serum albumin against heat and oxidative stress. Biochim. Biophys. Acta BBA - Proteins Proteomics, 1702, 9–17
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