[The determination of C-reactive protein by an immunoenzyme method].

The developed enzyme immunoassay of C-reactive protein is based on the use of a plane modified by a phosphorylcholine derivative lisolecithin. The method is highly sensitive (5-8 ng / ml), well reproducible; the correlation coefficients in measurements of blood serum C-reactive protein are compatible to results obtained by rocket immunoelectrophoresis and capillary precipitation: 0.94-0.

[Preparation of affinity sorbents for the isolation of phospholipase A2].

The preparation of biospecific organo-silica supports with different concentrations of covalently attached sn-glycero-3-phosphocholine was described. Sorbtion of phospholipase A2 on the hydrophobic analogues of biospecific supports was studied with the aim of elucidating the role of the enzyme-matrix hydrophobic interactions. A comparative characterization of the prepared sorbents was carried out.

[Isolation of phospholipase A2 on biospecific supports].

The procedure of isolation of phospholipase A2 from Agkistrodon halys blomhoffii venom and porcine pancreas on biospecific supports of an organo-silica type with immobilized phospholipid is described. The purity of isolated enzymes was controlled by polyacrylamide gel electrophoresis, determination of the N-terminal amino acid and isoelectrofocusing. The enzyme activity was equal to 80 mumole/mg/min and 1400 mumole/mg/min for snake venom phospholipase and for pancreatic phospholipase A2, respectively.