The ecology of environment nowadays

THE INFLUENCE OF PRESORBED WATER

ON THE SORPTION OF WATER VAPOUR, SILICON TETRAFLUORIDE, HYDROGEN CHLORIDE AND AMMONIA

ONTO GLOBULAR PROTEINS

G. N. Shikhaleeva, B. M. Kats

Physical Research Institute, University of Odessa,

 27 Pastera St., Odessa, 65026, Ukraine*

The equilibrium sorption of water vapour, silicon tetrafluoride, hydrogen chloride and ammonia on to globular proteins such as bull serum albumin (BSA), α-chymotrypsin (CHT), chymotrypsinogen (CHTG) and polysaccharide dextran T-20 was studied at the temperature 298 K.

It was shown that the preliminary hydration of biopolymers when exceeding the number of the surface charged groups of the side amino acid residua leads to the sharp sorption increase of hydrogen chloride and silicon tetrafluoride. It is established that for BSA, CHT, CHTG and dextran T-20 there exists the threshold hydration after which silicon tetrafluoride is actively sorbed as the result of hydrolysis.

It is founded out that the hydration of biopolymers containing SiF4 or HCl hemosorbed from the gaseous phase increases repeatedly.

The existence of the threshold value of the gaseous hydrogen chloride sorption was stated for the globular proteins (BSA, CHT and CHTG), and the further HCl sorption was proved not to depend on the nature of the sample.

It is also shown that the monolayer capacity (after Langmure) and the maximum capacity, estimated from the silicon tetrafluoride, hydrogen chloride and ammonia sorption isotherm, is several times less for polysaccharide dextran T-20 than the corresponding values of the globular proteins (BSA, CHT and CHTG).

It was shown that the value of hydrogen chloride and ammonia sorption can be used for the quantity estimation of the inorganic surface groups of the globular proteins (BSA, CHT and CHTG) side amino acid residua.

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