[Influence of coordination compounds of germanium (IV) and stannum (IV) on activity of some microbial enzymes with glycolytic and proteolytic action].

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.

[Biological activity of native and modified lipopolysaccharides Rahnella aquatilis].

The results of the comparative toxicity studies of native lipopolysaccharide (LPS) of Rahnella aquatilis 96U037 and that modified by tin complexes indicates that, due to the modification of LPS by tin complex with benzoylhydrazone of 4-dimethylaminobenzaldehyde, a decrease of its toxicity was observed that led to disappearance of the pyrogenic effect. All obtained derivatives lost completely the antigenic activity both in homologous and heterologous systems which may indicate to the interaction of modifying complexes with certain groups being the components of antigenic determinant. The paper is presented in Ukrainian.

[Characteristics of Aspergillus sp. 55 alpha-amylase].

The influence of different factors on biosynthesis of extracellular alpha-amylase of Aspergillus sp. 55 grown at submerged cultivation has been studied. The optimal composition of nutrient medium (1 g of starch and 0.5 g of NaNO3 per 1 l) was chosen. The enzyme preparation has a wide pH optimum of activity (4.5-9.0), thermooptimum at pH 6.5 was 60 degrees C, at pH 4.5 and 9.0--50 degrees C. The inhibitory effect of coordinative germanium compounds on amylolytic activity of the preparation was shown. The paper is presented in Ukrainian.

[Effect of coordination germanium compounds on biosynthesis and activity of proteases in Bacillus sp. and Yarrowia lipolytica].

The paper deals with the capacity of the coordination germanium compounds with citric acid in a complex with some aminoacids (aspartic acid, methionine, cysteine, threonine, phenylalanine, L-glutamic acid) as bioligands to affect synthesis and activity of the proteolytic enzyme complex of Bacillus sp. 27 and Yarrowia lipolytica 2061. Thus, biscitrategermanium acid H2[Ge(H4Citr)2] and its complex with aspartic acid (HAsp)2 [Ge(H4Citr)2] can be used with success for inducing biosynthesis ofcaseinolytic (182.1 and 197.4%) and elastase (182.6 and 383.3%) activities of Bacillus sp. 27, respectively. Biscitrategermanium acid can be used to induce biosynthesis of caseinolytic (182.1 and 197.4%) and elastase (182.6 and 383.3%) activities (respectively) of Bacillus sp. 27. Biscitrategermanium acid with methionine induced biosynthesis of caseinolytic (127.6%) and haemoglobinolytic (110.0%) activities of Y. lipolytica 2061. The tested coordinative compounds could not induce activity ofproteolytic complexes of both microorganisms. The capacity of complexes of citrategermanium acid with aspartic acid, methionine, cysteine, threonine, phenylalanine in concentration of 0.1% to inhibit activity of proteolytic complex of Y. lipolytica 2061 can be used in further studies of the catalytic centre of enzymes.

[The influence of coordinational germanium compounds on the activity of glycosidases].

The ability of the synthesized compounds of germanium with bioligands to affect the biosynthesis and activity of alpha-amylase and alpha-L-rhamnosidase has been studied. It was established the most complexes tested induced biosyntheis of alpha-amylase of Bacillus subtilis 147 (119-252%) with the exception of Pam (Pyracetam) and II (Ge-nicotinic-citric acid). At the same time the biosynthesis of alpha-amylase of Bacillus licheniformis 234 and alpha-L-rhamnosidase of Penicillium commune was inhibited by a number of synthesized compounds. The complexes IV (Ge-malonic acid) and VIII (Ge-nicotinamide-malonic acid) did not exert any effect on the biosynthesis of alpha-amylase however complex IV stimulated alpha-L-rhamnosidase biosynthesis on the 3rd day of producer cultivation. The study of influence of the studied germanium compounds on the activity of alpha-amylase and alpha-L-rhamnosidase gives every reason to suppose that they are the inhibitors of the above-mentioned enzymes.

[The biological activity of a lipopolysaccharide from Ralstonia solanacearum ICMP 7859 and of its modified derivative]. / Biologicheskaia aktivnost' lipopolisakharida Ralstonia solanacearum ICMP 7859 i ego modifitsirovannogo proizvodnogo.

Coordinational compound of the Ralstonia solanacearum ICMP 7859 lipopolysaccharide (LPS) with germanium was obtained. The derivative has lost to considerable extent its toxicity (as compared to the initial substance) but preserves immunomodulating activity, interferon-inducing one in particular. Lipid A modification has led to complete loss of interferon-inducing activity. Apparently, phosphate at C4' GlcN II can be responsible for interferon-inducing activity of lipid A, while carboxylic groups of core oligosaccharide or 0-specific polysaccharide, are responsible for that in native molecule of LPS.

[Optimization of culture conditions of Aspergillus niger for the synthesis of alpha-N-acetylgalactosaminidase and alpha-galactosidase]. / Optimizatsiia uslovii kul'tivirovaniia Aspergillus niger, sinteziruiushchego al'fa-N-atsetilgalaktozaminidazu i alfa-galaktozidazu.

Different factors have been investigated for their effect on the process of biosynthesis of alpha-N-acetylgalactosaminidase and alpha-galactosidase of Aspergillus niger under deep-water cultivation. Optimal sources and concentrations of carbon (soy flour--25 g/l) and nitrogen (pepton--7.5 g/l) were estimated. It has been established that temperature of 25 degrees C, pH 6.0, growing in 50 ml medium at the swing velocity 220 rev/min. for 6-8 days are optimal cultivation parameters. It has been shown that dry borine blood (in concentration of 1%) and a number of guanidine derivatives (guanidine carbonate--0.25%, nitroaminoguanison dimethylaminobenzaldehyde--0.05%, nitroaminoguanison of salicylic aldehyde--0.1%) can play the part of inducers of the mentioned glycosidase synthesis. When growing fungal culture in selected conditions synthesis of enzymes increased almost 3 times. Activity of alpha-N-acetylgalactosaminidase was 0.46 E/ml, and alpha-galactosidase--1.9 E/ml.

[Effect of coordinational germanium compounds on enzyme synthesis and activity]. / Vliianie koordinatsionnykh soedinenii germaniia na sintez i aktivnost' fermentov.

Germanium complexes (IV) with succinic (H2Suc), oxyethyliminodiacetic (H2Oeida) and iminodisuccinic (H4Ids) acids as well as homo- and heteroligand germanium complexes (IV)--products of interaction of triammonium salt of oxyethylidendiphosphonic acid ((NH4)3HL) and oxyacids: tartaric (H4Tart), citric (H4Citr), trioxyglutaric (H4Toglut) acids have been synthesized. Composition of the obtained complexes: [Ge(OH)2(NaSuc)2].2H2O (I); [Ge(OH) (Oeida).H2O].H2O (II); [Ge(OH)2(NaHIds)2] (III); [Ge(OH)2(NH4)3HL) (H2Tart)] (IV); [Ge(OH)2(NH4)3HL) (H2Citr)] (V); [Ge(OH)2(NH4)3HL) (H2Toglut)] (VI); [Ge(OH)2((NH4)2HL)2] (VII); [Ge (OH)2((NH4)2HL)2] (VII); [Ge(OH)2 (H2O)2(NH4) HL] (VIII) has been determined. The capability of the synthesized compounds has been studied to affect synthesis and activity of the following enzymes: collagenase, alpha-N-acetylgalactosaminidase (alpha-GalNAc-ase) and alpha-galactosidase (alpha-Gal-ase). It has been established that the complexes II-VIII activate biosynthesis of alpha-Gal-ase and alpha-GalNAc-ase, while germanium dioxide (IX) and complex I possess considerable inhibiting effect on synthesis of the above enzymes. It has been also established that all the compounds except for IV increased the activity of both alpha-Gal-ase and alpha-GalNAc-ase. All the considered complexes demonstrated similar reaction with respect to collagenase: they inhibited both synthesis and activity.

[The toxicity and interferon-inducing activity of the lipopolysaccharides of Cytophaga sp. (strains 81 and 92)]. / Toksichnost' i interferonogennaia aktivnost' lipopolisakharidov Cytophaga sp. (shtammy 81 i 92).

The experiments on mice and cell culture of a kidney of green monkey Vero have shown that lipopolysaccharides (LPS) of the studied strains 81 and 92 of Cytophaga sp. were nontoxic. They were less active as compared to LPS of other Gram-negative bacteria as to interferon-inducing activity. A comparative study of initial and dephosphorylated LPS has shown that phosphate groups were not responsible for the interferon-inducing activity of LPS of Cytophaga genus representatives.

[Complexes of cobalt (II, III) with derivatives of dithiocarbamic acid--effectors of peptidases of Bacillus thuringiensis and alpha-L-rhamnozidase of Eupenicillium erubescens and Cryptococcus albidus].

The influence of cobalt (II, III) coordinative compounds with derivatives of dithiocarbamic acid on Bacillus thuringiensis IMV B-7324 peptidases with elastase and fibrinolytic activity and Eupenicillium erubescens and Cryptococcus albidus alpha-L-rhamnosidases have been studied. Tested coordinative compounds of cobalt (II, III) on the basis of their composition and structure are presented by 6 groups: 1) tetrachlorocobaltates (II) of 3,6-di(R,R')-iminio-1,2,4,5-tetratiane--(RR')2Ditt[CoCl4]; 2) tetrabromocobaltates (II) of 3,6-di(R,R')-iminio-1,2,4,5-tetratiane--(RR')2Ditt[CoBr4]; 3) isothiocyanates of tetra((R,R')-dithiocarbamatoisothiocyanate)cobalt (II)--[Co(RR'Ditc)4](NCS)2]; 4) dithiocarbamates of cobalt (II)--[Co(S2CNRR')2]; 5) dithiocarbamates of cobalt (III)--[Co(S2CNRR')3]; 6) molecular complexes of dithiocarbamates of cobalt (III) with iodine--[Co(S2CNRR')3] x 2I(2). These groups (1-6) are combined by the presence of the same complexing agent (cobalt) and a fragment S2CNRR' in their molecules. Investigated complexes differ by a charge of intrinsic coordination sphere: anionic (1-2), cationic (3) and neutral (4-6). The nature of substituents at nitrogen atoms varies in each group of complexes. It is stated that the studied coordination compounds render both activating and inhibiting effect on enzyme activity, depending on composition, structure, charge of complex, coordination number of complex former and also on the enzyme and strain producer. Maximum effect is achieved by activating of peptidases B. thuringiensis IMV B-7324 with elastase and fibrinolytic activity. So, in order to improve the catalytic properties of peptidase 1, depending on the type of exhibited activity, it is possible to recommend the following compounds: for elastase--coordinately nonsaturated complexes of cobalt (II) (1-4) containing short aliphatic or alicyclic substituents at atoms of nitrogen and increasing activity by 17-100% at an average; for fibrinolytic--neutral dithiocarbamates of cobalt (II, III) (4-5) (by 29-199%). For increasing the fibrinolytic activity of peptidase it is better to use dibenzyl- or ethylphenyldithiocarbamates of cobalt (III), which increase activity by 15-40% at an average. The same complexes, and also compound {(CH2)6}2Ditt[CoCl4] make an activating impact on alpha-L-rhamnosidase C. albidus (by 10-20%).

[Biological activity of native and modified lipopolysaccharides of Pragia fontium].

Modified lipopolysaccharides (LPS) of Pragia fontium were obtained with germanium complexes (IV) of 2-aminobenzoylhydrazon of salicylic aldehyde (2-NH2-H2Bs), 2-hydroxybenzoylhydrazon salicylic aldehyde (2-OH-H2Bs) and nicotinoylhydrazon of salicylic aldehyde (H2Ns). The modification of LPS was confirmed by IR spectroscopy. Comparative investigations of pyrogenic activity of native and modified LPS showed, that only P. fontium 20125 LPS, modified by germanium complexes with 2-hydroxybenzoylhydrazon of salicylic aldehyde (2-OH-H2Bs) has lost the pyrogenic activity. In the homological reactions of double immunodiffusion in agar it was shown that all modified LPS unlike the native ones lose completely antigenic activity.

[Induction of synthesis and activation of Penicillium commune alpha-L-rhamnosidase].

For the first time the influence of a number of synthetic porfirin and fluoren derivatives, coordinative germanium substances and surfactants on the biosynthesis and activity of Penicillium commune 266 alpha-L-rhamnosidase has been studied. It is shown that some of porfirin derivatives and coordinative germanium substances may be used as inducers of biosynthesis (143-430%) and also as stimulators of alpha-L-rhamnosidase activity (15-44%). It is more expedient to use biscitratgermanium acid in a complex with asparaginic acid (430%) or threonine (370%) as inducers of biosynthesis of enzyme. At the same time the use of porfirin derivatives, in particular meso-tetra(N-methyl-6-chinoline)porfirin tosilate or its manganese complex, is more efficient as stimulators (40%) of alpha-L-rhamnosidase activity. The utilization of such surfactants as tregaloso-, peptido- and rhamnolipids is not expedient. These compounds either do not influence or inhibit biosynthesis and activity of P. commune alpha-L-rhamnosidase. Only in concentration of 0.01% rhamnolipid increased the activity of enzyme by 7.5%.