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J Turková

Publications and source records attributed to J Turková.

28 records · Page 2Linked to original sources
PubMedDate not supplied

Detection of pathological changes of proteins by peptide mapping after protein digestion by use of oriented immobilized proteinases.

Diagnostic methods for detecting gastric diseases using chymotryptic digestion of pepsin are discussed. Peptide maps can be prepared using reversed-phase high-performance liquid chromatography. Batchwise chromatography by use of membranes with immobilized Tyr(I2) was used for the isolation of pepsin from gastric mucosa extract or from human blood serum. Enzymes immobilized using suitable antibodies or through their sugar moieties can be used for the preparation of peptide maps because such enzymes share good steric accessibility to their active binding sites and possess increased thermal stability. Biospecific adsorption of proteins to immunosorbents combines the simultaneous isolation of these enzymes with their oriented immobilization. Proteins were stabilized by hydrophilization through the attachment of saccharide residues containing galactose residues. These residues could be activated by oxidation using galactose oxidase and subsequently immobilized to hydrazide-containing solid supports.

Chromatography↗
PubMedDate not supplied

Hydrazide-functionalized poly(2-hydroxyethyl methacrylate) microspheres for immobilization of horseradish peroxidase.

Nonporous cross-linked poly(2-hydroxyethyl methacrylate-co-ethylene dimethacrylate) (poly(HEMA-co-EDMA)) microspheres were prepared by dispersion polymerization of HEMA and EDMA. The polymerization was performed in toluene/2-methylpropan-1-ol in the presence of cellulose acetate butyrate as a steric stabilizer and dibenzoyl peroxide initiator. The particle size may be increased by decreasing the toluene/2-methylpropan-1-ol ratio and by increasing polymerization temperature. Adipohydrazide was attached to the microspheres activated with 2,4,6-trichloro-1,3,5-triazine. After periodate oxidation of its carbohydrate moieties, horseradish peroxidase was coupled to the hydrazide-functionalized poly(HEMA-co-EDMA) microparticles up to 7.3 microgram of enzyme/g of carrier without a significant loss of its activity. Immobilized peroxidase was found to be stable, retaining more than 97% of its initial activity when stored for 23 days after the preparation.

Cross-Linking Reagents↗