[Chemiluminescence fiber optic immunosensor for detecting antibodies to the influenza virus]. / Khemiliuminestsentnyi optovolokonnyi immunosensor dlia opredeleniia antitel k virusu grippa.

A new variant of an optoimmunosensor for determination of antibodies to the influenza virus has been elaborated. Its advantages as compared to the traditional solid phase immunoenzyme analysis in respect to sensitivity and expressiveness are demonstrated. Time of the sensor response is below 17 min. When analyzing the 1:320 diluted serum, about 80% of response value is implemented after 6 min. Optimum conditions of the optoimmunosensor transducer regeneration are chosen. They permit reusing it for 20-30 cycles of measurements. A conclusion is made on the prospects of the developed variant of the optosensor for the immunoanalysis of antigens and antibodies under the equilibrium and kinetic conditions.

[A method of solid phase immunoenzyme analysis using antigen molecules immobilized on membranes]. / Metod tverdofaznogo immunofermentnogo analiza s ispol'zovaniem immobilizovannykh na membranakh molekul antigena.

The enzyme-linked immunoassay modification has been worked out. The method combines advantages of membrane technology of antigen immobilization which is used in the enzyme immunosensory technique and of conventional enzyme-linked immunosorbent assay. The nitrocellulose and polypropylene membranes are used as a solid-phase. The purified rabbit immunoglobulin G is immobilized on the surface of membranes as the first layer. The competitive immunoassay is employed. The immunoglobulin G concentration range is 1-1000 ng/ml. The membranes with the immobilized antigen can be repeatedly used after incubation in 0.1 M glycine buffer, pH 2.5. The dry membrane with the immobilized antigen can be used after keeping for 6 months in refrigerator at 4 degrees C without changing the concentration range measured.

[The lactate oxidase activity of Aerococcus viridans cultures]. / Laktatoksidaznaia aktivnost' kul'tur Aerococcus viridans.

The oxidase activity of Aerococcus viridans is a result of the functioning of aerobic NAD-independent lactate dehydrogenase. Two fractions of flavin-containing protein which oxidize D- and L-isomers of lactic acid are revealed during the enzymic complex electrophoresis in PAAG. The enzymic complex and eluates of both fractions possess the antagonistic activity relative to 27 test-cultures of bacteria.