抄録
Heating followed by freezing and frozen storage of acid-precipitated protein caused an increase in the hardness of its gel in the presence of cetyltrimethylammonium bromide, acetylcholine bromide, choline chloride, and phosphatidylcholine dipalmitoyl, which all contain trimethylammonium residue. A comparison of the effect of choline chloride and ethanolamine chloride (a primary amine) suggests that trimethylammonium residue contributes to gel formation. When N-ethylmaleimide (NEM) was present, neither gel formation nor any action of trimethylammonium residue-containing compounds was observed. This result suggests that these compounds accelerate
interaction among the subunits through sulphydryl-disulphide interchange.
