[Biochemical and photochemical degradation of the herbicide lontrel].

Degradation of Lontrel by activated sludge (AS) of purification works and UV irradiation was studied. 3,6-Dichloropicolinic acid (3,6-DCPA, the main active principle of Lontrel) was not degraded by the microbial association of the AS. AS treated with nitrosourea under various conditions did not oxidize Lontrel either. Hard UV radiation degraded 3,6-DCPA within 4-24 h at constant sparging (bubbling) of air, oxygen, or ozone. The rate of oxidation with oxygen or ozone bubbling was three to four times higher than with air bubbling. It was found that the products of photochemical degradation of Lontrel were also toxic; however, they were readily degraded by AS microorganisms without additional AS treatment.

[Immobilization of phosphorylase B and study of its enzymatic and immunological properties]. / Immobilizatsiia fosforilazy b i izuchenie EE fermentativnykh i immunologicheskikh svoistv.

The properties of phosphorylase B (PhB) immobilized on an agar derivative were studied. It was shown that the enzyme activity makes up to 15-20% as compared to that of the soluble enzyme, the Km value for glucose-1-phosphate is increased 1.5-fold and the pH optimum remains unchanged, whereas the thermostability of enzyme shows a considerable increase. PhB immobilized on a highly activated sorbent completely losses its enzymatic activity but retains its antigenic properties and binds 1.6-2 mol antibodies (per monomer). Using immunosorbents, purified antibodies homogeneous during electrophoresis in polyacrylamide gel were isolated. The immunosorbent capacity is 500-800 mg of antibodies per 1 g of dry weight. The purified antibodies are characterized by a lower inhibitory power upon interaction with soluble PhB. The type of inhibition of both immobilized and soluble enzyme is similar. It is assumed that immobilization produces conformational changes only at the active site of enzyme, which is spatially separated from the antibody binding site.