The proteins concerned have been spread at the air/water interface on a substrate at physiological ionic strengths. Spread protein
A
has been ‘injected’ with dissolved protein
B
, and the increase in pressure observed has been attributed to adsorption. This adsorption has been found to depend on the area per molecule of the spread protein, reaching a maximum value at an intermediate area value. It is postulated that adsorption occurs by hydrogen bonds between
B
and
A
, and that at a certain stage of compression the bonding groups in
A
turn so as to form hydrogen bonds
within
the monolayer, a theory which accords with compressibility and viscosity data on the monolayers. The rate of increase of pressure depends markedly on ionic strength suggesting that the rate of adsorption is influenced by the interaction of ionic groups in
A
and
B
. No evidence was obtained for a surface clotting reaction or specific interaction between fibrinogen and thrombin, whichever protein formed the monolayer, suggesting that the specific interaction involves at least two groups in each protein held at a critical spacing.
Bridging the relationship between energy benefit of waste incineration and risk of trace persistent organic pollutant emissions