Regulation of acid phosphatase in reverse micellar system by lipids additives: structural aspects.

Reverse micelles system is suggested as a direct tool to study the influence of membrane matrix composition on the activity and structure of membrane-associated enzymes with the use of acid phosphatase (AP) as an example. In reverse micelles the functioning of the monomeric and dimeric forms of AP could be separately observed by variation of the size of the micelles. We found that including the lipids into the micellar system can dramatically affect the enzyme functioning even at low lipid content (2% w/w), and this effect depends on the lipid nature. Structural studies using CD spectroscopy and DLS methods have shown that the influence of lipid composition on the enzyme properties might be caused by the interaction of lipids with the enzyme as well as by the influence of lipids on structure and properties of the micellar matrix.

Regulation of catalytic activity of acid phosphatase by lipids in a reverse micellar system.

The influence of biomembrane lipids on the catalytic activity of a peripheral membrane enzyme, acid phosphatase (AP), was studied in a reverse micellar system. It was found that the interaction of AP with lipids led to a number of kinetic effects depending on lipid nature on enzyme function. The observed effects might be caused by the formation of lipoprotein complexes as well as by the influence of lipids on structure and properties of the micellar matrix. The results are important for clear understanding of molecular mechanisms of regulation of the catalytic activity of the membrane-associated enzyme in vivo. These data can also be used as a physicochemical basis for application of AP in medical fields as a diagnostic tool for diseases caused by changes in lipid metabolism, e.g. urinary, orthopedic, and allergic diseases.