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Interaction of detergents with transfusion gelatin
Author(s) -
Malik W. U.,
Ashraf S. M.
Publication year - 1970
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02531395
Subject(s) - gelatin , micelle , chemistry , dialysis , sodium , chromatography , molecule , aqueous solution , biochemistry , organic chemistry , medicine
Binding of sodium dodecyl and octyl sulphate to transfusion gelatin has been studied at pH 7.7 by equilibrium dialysis. At lower detergent concentration the binding is statistical, whereas at higher concentrations the binding increases apparently without limit. This may be explained by assuming unfolding of the protein molecule with formation of detergent micelles around the binding sites.