Abstract
Evans blue has been demonstrated to promote the autolysis of α-chymotrypsin at low dye-to-protein ratios in alkaline solution. This effect has been attributed to the stabilization of less tightly folded conformers of the protein by the dye. The effect is specific. Of 20 other strongly acidic dyes tested, only trypan red showed activity comparable to that of Evans blue. A general discussion of the influence of ligand binding on the stability of proteins is presented.
Full text
PDF





Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Citri N., Zyk N. The interaction of penicillinase with penicillins. IV. Structural aspects of catalytic and non-catalytic interactions. Biochim Biophys Acta. 1965 Jun 22;99(3):427–441. doi: 10.1016/s0926-6593(65)80197-7. [DOI] [PubMed] [Google Scholar]
- GRISOLIA S. THE CATALYTIC ENVIRONMENT AND ITS BIOLOGICAL IMPLICATIONS. Physiol Rev. 1964 Oct;44:657–712. doi: 10.1152/physrev.1964.44.4.657. [DOI] [PubMed] [Google Scholar]
- Glazer A. N. The specific binding of Biebrich Scarlet to the active site of alpha-chymotrypsin. J Biol Chem. 1967 Oct 10;242(19):4528–4533. [PubMed] [Google Scholar]
- LEESON D., REEVE E. B. A method for testing the purity of commercial samples of T 1824 with observations on the amounts of colored impurities present and the errors in plasma volume estimation caused by them. J Physiol. 1949 Aug;109(1-2):170–176. doi: 10.1113/jphysiol.1949.sp004382. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Markus G. Protein substrate conformation and proteolysis. Proc Natl Acad Sci U S A. 1965 Jul;54(1):253–258. doi: 10.1073/pnas.54.1.253. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SCHONBAUM G. R., ZERNER B., BENDER M. L. The spectrophotometric determination of the operational normality of an alpha-chymotrypsin solution. J Biol Chem. 1961 Nov;236:2930–2935. [PubMed] [Google Scholar]
