The influences of anhydrous hydrogen fluoride on the native form of hen egg-white lysozyme under standard conditions of peptide synthesis were investigated by measuring the enzymatic activities of materials recovered from mixtures of anhydrous hydrogen fluoride and hen egg-white lysozyme. The enzymatic activity of hen egg-white lysozyme gradually decreased on incubation with anhydrous hydrogen fluoride at a given temperature. After incubation of the mixture at 0 °C for 60 min, at least three fractions could be separated by gel-filtration on Sephadex G-50. One of these was eluted in the same position as native lysozyme and was fully active enzymatically. Its ultra-violet, and circular dichroism absorptions were identical with those of native lysozyme, and the tetragonal crystals obtained from this fraction could not be distinguished from those of native lysozyme.
No takes yet. Share an insight, caveat, or question.
Aimoto et al. (1975) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: