ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)
"Biotechnologia Acta" V. 8, No 4, 2015
https://doi.org/10.15407/biotech8.04.082
Р. 82-91, Bibliography 30, English
Universal Decimal Classification: 541.49:546.47
Nidialkova N. А.1, Varbanets L. D.1, Seifullina І. I.2, Shmatkova N. V.2
1Zabolotny Institute of M Varbanets icrobiology and Virology of the National Academy of Sciences of Ukraine, Kyiv
2Mechnikov Odesa National University
The purpose of the research was to investigate the influence of stanum (IV) and germanium (IV) coordination compounds on peptidases 1 and 2 of Bacillus thuringiensis var. israelensis ІМV В-7465 activity. The study of coordination compounds effect on peptidase activity was carried out by complexes with the enzymes incubation and residual activity to the collagen, elastin and fibrin determination. It was revealed the regularity in the influence of different structure complex compounds on peptidases of B. thuringiensis var. israelensis ІМV В-7465 activity. The stanum (IV) complexes with salicyloylhydrazones of aromatic aldehydes increase collagenase and elastase activities. Substituents replacement in aldehyde fragment of stanum (IV) with isonicotinoylhydrazones of aromatic aldehydes complexes by the less polar ones contributed to increase of elastase activity of both enzymes while an absence of substituents enables to increase peptidase 2 fibrinolytic activity. The complexes of germanіum (IV) with isonicotinoylhydrazone of salicylic aldehyde which contain Zn and Co, increased collagenase activity of the peptidase 1 as well as elastase and fibrinolytic activities of the peptidase 2. In general, all tested complexes may be considered as peptidase effectors of B. thuringiensis var. israelensis ІМV В-7465. A difference of complexes effect on activities of the both enzymes is due to the characteristics of the structure of coordination compounds.
Key words: stanum (IV) and germanіum (IV) complexes with salicyloyl- and sonicotinoylhydrazones of aromatic aldehydes, peptidases with collagenase, elastase and fibrinolytic activity.
© Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 2008
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