[Selective photoimmunoinactivation of influenza virus].

Antibodies to influenza virus were conjugated with hematoporphyrin. The conjugates were verified by the peak point identity in protein absorption (lambda-280 nm) of elution profiles and by the porphyrin-specific fluorescence. The antibody conjugates have been shown to preserve the specific antigenic activity tested by enzyme immunoassay.

[Interaction of rabbit skeletal muscle glycogen synthase I with substrate analogs--oxo-UDP hydrazones].

Inhibition of rabbit skeletal muscle glycogen synthase I was studied by using several synthetic substrate analogs: dansylhydrazone of oxo-UDP, 3-hydroxy-2-naphthoylhydrazone of oxo-UDP, salicyloylhydrazone of oxo-UDP, 1-oxyl-2,2,5,5-tetramethylpyrrolidine-3-carbonylhydrazone of oxo-UDP, N'-(dansyl)hydrazinocarbonylhydrazone of oxo-UDP and N'-(fluorenylidene-9)-hydrazinocarbonylhydrazone of oxo-UDP. All these compounds (with the exception of the nitroxyl-containing hydrazone) were characterized by a nonlinear dependence of the reverse reaction rate on the analog concentration in Dixon coordinates. The parabolic type of inhibition was due to the fact that the analogs tested except for the nitroxyl-containing hydrazone were able to interact both with the active center of the enzyme and with the FMN-binding site.

[Interaction of glycogen synthase from rabbit skeletal muscles with 1,5-gluconolactone].

1.5-Gluconolactone was shown to inhibit in a competitive manner the activity of both I- and D-forms of rabbit skeletal muscle glycogen synthase. Unlike other known inhibitors (UDP and adenyl nucleotides) the affinity of the enzyme D-form for 1.

[Inhibition of glycogen synthase I from rabbit skeletal muscles by 1,5-gluconolactone].

The effect of 1.5-gluconolactone on the activity of rabbit skeletal muscle glycogen synthase I was investigated. Using statistic methods (pair regressive analysis) and computer analysis on a Robotron EC 1834 personal computer, it was found that 1.

[Turbidimetric method of determination of glycogen synthase activity in rabbit skeletal muscles].

A turbidimetric procedure is described, which involves the monitoring of changes in glycogen turbidity at wavelengths above 300 nm and continuous recording of rabbit skeletal muscle synthase activity. The recalculation coefficients were found to be equal to 1.69 +/- 0.