Sorption of water vapour by some derivatives of bovine serum albumin

Abstract

Isotherms for the sorption of water vapour by succinyl, acetyl, amidino, methyl and carbodiimide derivatives of bovine serum albumin at 298 K have been determined gravimetrically. The effects of the specific chemical modifications on the uptake of water by B.S.A. are discussed by consideration of the groups in the protein which are possible sites for water sorption. Adsorption onto both side chain polar or ionic groups and chain peptide groups occurs. Release of main chain peptide groups from the α-helical conformation enhances their capacity to sorb water.