[Influence of coordination compounds of germanium (IV) and stannum (IV) on activity of some microbial enzymes with glycolytic and proteolytic action]
| Autor: | L D, Varbanets', O V, Matseliukh, N A, Nidialkova, O V, Hudzenko, K V, Avdiiuk, N V, Shmatkova, I Ĭ, Seĭfullina |
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| Rok vydání: | 2015 |
| Předmět: |
Glycoside Hydrolases
Germanium Bacillus thuringiensis Hydrazones Microbial Sensitivity Tests NAD Fungal Proteins Cryptococcus Structure-Activity Relationship Anti-Infective Agents Bacterial Proteins Coordination Complexes Tin Benzaldehydes Eupenicillium Organotin Compounds Aspergillus flavus Peptide Hydrolases |
| Zdroj: | Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993). 76(6) |
| ISSN: | 1028-0987 |
| Popis: | Influence of coordinative compounds of germanium (IV) and stanum (IV) (complexes of germanium (IV) with nicotinamide (Nad) [GeCl2(Nad)4]Cl2 (1) and complexes of stanum (IV) with 2-hydroxybenzoilhydrazone 4-dimetylaminobenzaldehide (2-OH-HBdb) [SnCl4(2-OH-Bdb-H)] (2), 3-hydroxy-2-naphtoilhydrazone 2-hydroxynaphtaldehide (3-OH-H2Lnf) [SnCl3(3-OH-HLnf)] (3) and izonicotinoilhydrazone 2-hydroxyibenzaldehide [SnCl3 (Is·H)] (4) on activity of peptidases 1 and 2 Bacillus thuringiensis, α-L-rhamnosidase Cryptococcus albidus, Eupenicillium erubescens and α-amylase Aspergillus flavus var. oryzae. Results testify that all studied compounds differ on their influence on activity of the enzymes tested: significantly don't change elastolytic activity of peptidases 1 and 2 B. thuringiensis, completely inhibit A. flavus var. oryzae amylase, activate or oppress of α-L-rhamnosidase C. albidus and E. erubescens. Considerable differences in compounds (3, 4) on activity observed in case of the last. It's possible that peculiarity of influence (1) in compare with (2-4) is connected with existence of different central atoms of complexants: germanium (IV) (1) and stanum (IV) (2-4). A certain analogy in oppression of C. albidus α-L-rhamnosidase by compounds (1) and (4) can explain with presence of a pyridinic ring at molecules of their ligands. The less activsty displayed compound (2) with coordinative knot {SnCl4ON}. Nature of compounds (3, 4) activity was absolutely different: essential increase of activity of C. albidus α-L-rhamnosidase and full oppression of E. erubescens α-L-rhamnosidase by compound (3), while the action of compound (4) was feed back. Taking into account identical coordination knot {SnCl3O2N} the major role in this case play change of a hydrazide fragment in molecules of their ligands. |
| Databáze: | OpenAIRE |
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