[The optical biosensor study of the redox partners interactions within the cytochrome P450 2B4-containing monooxygenase system in hydroxylation conditions].

Interactions between cytochrome P450 2B4, NADPH:cytochrome P450 reductase and cytochrome b5 have been investigated in the presence of a substrate (7-pentoxyresorufin) and an electron donor, NADPH, in the monomeric reconstituted P450 2B4-contained monooxygenase system. Each partner was immobilized via its amino groups on the carboxymethyldextran biochip surface of an optical biosensor IAsys+. It was shown that, despite immobilization of any of the partners (via their respective amino groups) onto the carboxymethyldextran surface of the IAsys+ optical biosensor, its activity didn't loss.

[Isolation and structure of peptides from oat (Avena sativa) seedlings].

The level of proteolytic activity in tissues of oat seedlings was characterized under acidic conditions, and the number and content of the main components in low-molecular-mass fractions of the extract were determined. The structures of the majority of predominant peptide components isolated from the extract were studied. The use of a database of protein structures helped suggest possible structures of protein precursors of the peptides isolated.