The binding of anionic and nonionic surfactants to collagen through the hydrophobic effect
- 1 April 1991
- journal article
- research article
- Published by Springer Nature in Protein Journal
- Vol. 10 (2), 189-192
- https://doi.org/10.1007/bf01024783
Abstract
The adsorption of nonionic surfactants on hide powder previously treated with anionic surfactants has been studied. The adsorption of nonionic surfactants takes place through hydrophobic interactions. A mechanism has been proposed for this interaction, assuming that the nonionic surfactant has been fixed by means of secondary adsorption (hydrophobic interaction) after the primary adsorption of the anionic surfactant (ionic and hydrophobic interaction) which makes it possible.This publication has 7 references indexed in Scilit:
- Biochemistry of CollagenPublished by Springer Nature ,1976
- Nonspecific large binding of amphiphiles by proteinsBiochemistry, 1974
- The Interaction of a Cationic Detergent with Bovine Serum Albumin and Other ProteinsJournal of Biological Chemistry, 1974
- Differences between bovine and human serum albumins. Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effectsBiochemistry, 1971
- The Binding of Divers Detergent Anions to Bovine Serum Albumin*Biochemistry, 1967
- The amino-acid composition and titration curve of collagenBiochemical Journal, 1948
- A new method for the rapid titrimetric analysis of sodium alkyl sulphates and related compoundsTransactions of the Faraday Society, 1948