Publications by authors named "S A Kurzeev"

Article Synopsis
  • A new assay was developed to measure the activity of the nicking endonuclease (NE) Nt.Bst9I using biotinylated DNA oligonucleotides as a substrate.
  • To enhance the assay's sensitivity, a chemiluminescent detection system was implemented, utilizing a streptavidin-polyperoxidase conjugate and an enhanced chemiluminescence reaction.
  • The assay methods were designed for microtiter plates, facilitating automated analysis with ELISA equipment, and the heterogeneous format proved to be more sensitive than the homogeneous-heterogeneous format.
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Sensitive microplate-based chemiluminescent assay coupled with isothermal circular strand-displacement polymerization reaction (ICSDPR) for DNA detection was developed. The assay sensitivity was improved using a triple amplification strategy based on employment of ICSDPR, streptavidin-polyperoxidase conjugate and an enhanced chemiluminescent reaction. To increase the accuracy all stages of the assay (one-pot format) were carried out in the same microplate well.

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Laccases are multicopper oxidases that catalyze oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. The physicochemical and catalytic properties of two new fungal laccases from basidiomycetes Antrodiella faginea (AfL) and Steccherinum murashkinskyi (SmL) with middle redox potential of the T1 copper site were studied. The X-ray structures of AfL and SmL were solved at 1.

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Gene egl2 of secreted endo-(1-4)-beta-glucanase of glycosyl hydrolase family 5 of the mycelial fungus Penicillium canescens was cloned. The gene was expressed in P. canescens under control of a strong promoter of the bgaS gene encoding beta-galactosidase of P.

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This paper describes the structural analysis of the native form of laccase from Trametes hirsuta at 1.8 A resolution. This structure provides a basis for the elucidation of the mechanism of catalytic action of these ubiquitous proteins.

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