[Nucleotide sequence of the B1-hordein gene of barley Hordeum vulgare L]. / Nukleotidnaia posledovatel'nost' gena B1-gordeina iachmenia Hordeum vulgare L.

The gene encoding B1 hordein of Hordeum vulgare (cv. Donetsky 4) was cloned and entirely sequenced. It contains no introns and codes for of 293 amino acids long polypeptide with molecular weight 33418. Our clone differs from the previously sequenced B1 hordein genes in some positions within the coding region (there are 4 nucleotide changes and a 12 bp deletion, as compared with the pB11 cDNA clone, and 5 nucleotide changes, as compared with the pBHP184 genomic clone). These changes result in polymorphism of amino acid sequences at 5 positions. 5'-flanking region contains putative regulatory and promoter sequences and differs from that of the pBHP184 clone in 3 positions.

[Study of patulin by NMR and mass spectroscopy]. / Izuchenie patulina metodami IaMR i mass-spektroskopii.

Patulin was studied by NMR and mass spectrometry. On the basis of the 1H and 13C NMR spectral analysis and experiments on double homo-(1H NMR) and heteronuclear (13C NMR) resonances complete assigning of the proton and carbon signals was achieved. Patulin was studied mass spectrometrically with using high performance mass spectrometry and the DADI technique. It was shown that formation of the [M--C2H4O]+ ion was due to rearrangement of the molecular ion (M+).

[Structure of the reaction adduct of xanthothricin with acetone]. / Stroenie addukta reaktsii ksantotritsina s atsetonom.

Reaction of xanthothricin demethylation by amines in acetone as a solvent yielded a new compound with a formula of C10H13N5O3. Mass spectrometry, 1H NMR-spectroscopy and x-ray analysis showed that the compound was 4H-1,6-dimethyl-4a(2-oxopropyl)-pyrimido-[5,4-e]-1 ,2,4-triazine-5,7-dione.

[Study of alkaline hydrolysis of reumycin using NMR spectroscopy]. / Izuchenie shchelochnogo gidroliza reumitsina metodom spektroskopii IaMR.

The transformation sequence of reumycin in aqueous (D2O) solutions with various pD was studied by NMR spectroscopy and the structures of the yielding products were determined. It was shown that formation of 6-(3-methylureido)-1,2,4-triazine-5-carboxylic acid was the first stage of reumycin alkaline hydrolysis. The subsequent cyclization of this compound resulted in obtaining 5-methyl-5H-imidazo [4,5-e]-1,2,4-triazin-6 (7H) one-4a-carboxylic acid in mono-,di- or trianionic form which depended on the medium pH and was due to dissociation of the carboxylic group, N(4)H group of the triazine ring and N(7)H group of the imidazolidinone ring.

[The antibiotic galtamycin. The structure of galtamycinone]. / Antibiotik galtamitsin. Stroenie galtamitsinona.

The structure of galtamycinone, a chromophore moiety of galtamycin, a new antitumor antibiotic was determined by spectral analysis, i.e. UV, NMR and mass spectrometry. Galtamycinone was shown to be 1,4,6-trioxy-10 [4 (e), 5 (e)-dioxy-6 (e)-methyl-tetrahydropyran-2(e)-yl]-8-methyl tetracendion-5,12. It represents a new type of anthracycline chromophores containing a C-glycoside bond in its molecule.

[Dehydration of aklavinone, PMR spectra of aklavinone and its dehydration products]. / Degidratatsiia aklavinona, spektry PMR aklavinona i produktov ego degidratatsii.

The PMR 1H spectra of aklavinone, monoanhydroaklavinone and bisanhydroaklavinone were completely assigned with the use of the double resonance technique and the method of resolution enhancement (multiplication of the free induction decay by the Gauss function). It was shown that under mild conditions in the presence of hydrazine, aklavinone dehydrated at the C9-C10 bond and transformed into monoanhydroaklavinone. Under less mild conditions when akalavinone was heated at 250 degrees C, dehydration proceeded at the C9-C10 and C7-C8 bonds to form bisanhydroaklavinone.

[Study of the stability of pyrimido-[5,4-e]-1,2,4-triazine antibiotics in acid-base media by NMR spectroscopy]. / Izuchenie ustoichivosti pirimido-[5,4-e]-1,2,4-triazinovykh antibiotikov v kislotno-osnovnykh sredakh metodom spektroskopii IaMR.

A comparative study of the NMR 1H and 13C spectra of reumycin, fervenulin and xanthothricin in aqueous acid-base media showed that at pH or pD ranging from 8.0 to 1.0 the antibiotics were chemically stable. By the ratio of the 1H and 13C chemical shifts of reumycin at pH 4.0-10.0 the pKa values of this antibiotic were determined: 6.7 in aqueous (D2O) solution and 8.76 in dimethylsulfoxide media. Alkalization of the solutions of reumycin (pH 12.0), fervenulin (pH 9.0) and xanthothricin (pH 8.0) resulted in irreversible chemical transformation of the antibiotics. The analysis of the chemical shifts in the PMR spectra of the transformation products revealed transformation of the uracil ring in reumycin and uracil and triazine rings in fervenulin and xanthothricin. Alkalization of the xanthothricin solutions resulted also in demethylation with formation of reumycin.

[Changing number of histone structural genes in Drosophila]. / Izmenenie chisla strukturnykh gistonovykh genov u drozofily.

It has been shown in the previous paper that if one Drosophila chromosome lacks histone genes, the intact homologous chromosome has an increased number of histone genes. The present study shows that the extent of compensatory multiplication of histone genes depends on the nature of the deficient chromosome. An extra Y chromosome in the genome of flies without the deficiency does not affect their histone gene content. In heterozygotes with a deficiency of histone genes the number of these genes grows gradually and reaches 90% of the norm in the eight generation (magnification). After the deficient chromosome is eliminated the increased number of histone genes is not stably inherited and reverts to the normal level in the course of 5--7 generations. Deficiency-heterozygous males of the first generation contain extrachromosomal histone DNA and have a changed ratio of the two types of histone gene blocks. The multiplication of histone genes is compared with the compensation and magnification of rDNA.

[Repetitious DNA in the genome of Drosophila lummei Hackman and its role in replication and chromosome behavior in mitosis]. / Povtoriaiushchaiasia fraktsiia DNK v genome Drosophila lummei Hackman, vliiaiushchaia na replikatsiiu i povedenie khromosom v mitoze.

The toromere previously found by other workers in the distal end of the sixth chromosome (microchromosome) of D. lummei was studied using differential staining of D. lummei giant chromosomes. The toromere which was first described as a quinacrine-bright structure appears as a C-positive body. Quantitative cytofluorometric analysis showed a significant increase in toromeric DNA under low temperature conditions. In situ hybridization of 125I nick-translated D. virilis sDNA (all three satellites were included in the sample) with polytene chromosomes of D. lummei larvae cultured at 12 degrees C revealed no label incorporation into the toromere region. However in situ hybridization of [3H]RNA complementary to highly repetitious DNA of D. lummei and D. virilis (C0t = 10(-1)--10(-2)) with polytene chromosomes of the larvae cultured at 12 degrees coupled with banding studies enable us to conclude that the toromere probably contains AT-rich repeated DNA. Well-developed toromere in the sixth chromosome of D. lummei was also demonstrated at normal temperature (25 degrees) in interspecific hybrids. The role of the toromere structure in the mitotic behaviour of microchromosomes and their replication pattern is discussed.

[Identification of the antibiotic formed by a Str. canulus 106/78 culture with antibiotic CC-1065]. / Identifikatsiia antibiotika, obrazuemogo kul'turoi Str. canulus 106/78, s antibiotikom CC-1065.

An antibiotic with a melting point of at least 340 degrees C, [alpha]D + 100 degrees (c 1 per cent in dimethylformamide) was isolated from the mycelium of Str. canulus 106/78. Calculated (%): C 60.63, H 4.69, N 13.6. The UV spectrum of the antibiotic (in methanol solution) showed the terminal absorption, shoulder at 265 nm and maximum at 375 nm. In dimethylformamide solution the UV absorption maximum was observed at 370 nm with E1 1% cm 845. The IR, FMR and 13C-NMR spectra of antibiotic 106 are analogous to the respective spectra of antibiotic CC-1065 which is indicative of their identity.

[Effect of the deficiency of histone structural genes on their amount in Drosophila]. / Vliianie nekhvatki gistonovykh genov na ikh kolichestvo u drozofily.

The amount of histone structural genes was determined in heterozygotes for two different deficiencies of the histone locus of the 2nd chromosome. In case one chromosome lacks histone genes, the number of histone structural genes in the normal homologous chromosome is likely to increase by means of magnification and compensation in the same way as in the case of rRNA genes.

[Streptomycin-3"-phosphotransferases from streptomycin-resistant cells of Escherichia coli strains]. / Streptomitsin-3"-fosfotransferazy iz kletokh ustoichnvykh k streptomitsinu shtammov Escherichia coli.

Streptomycin-3"-phosphotransferases were isolated and purified from E. coli cells containing plasmids 836, pBS52 or R6K, which determine the microorganisms resistance towards streptomycin and dihydrostreptomycin. Phosphorylation of the 3"-hydroxylic group of dihydrostreptomycin was demonstrated by [13C]-NMR spectrometry. It was shown that streptomycin-3"-phosphotransferase, whose synthesis is determined by plasmid 836 (as well as by plasmid R6K), differs from the analogous enzyme, whose synthesis is operated by plasmid pBS52 in some properties, e. g. dependence of the initial reaction rate on concentrations of antibiotics and ATP, pH-optimum, sensitivity to the buffer ionic strength, stability, etc. Besides, the antiserum against streptomycin-3'-phosphotransferase detected by plasmid pBS52 does not produce cross immunological reactions with the other enzyme.

Increase in the number of histone genes in case of their deficiency in Drosophila melanogaster.

We have determined the number of histone structural genes in D. melanogaster heterozygotes for two different deficiencies of a histone locus in the 2d chromosome. The results indicate a possibility of histone genes increasing in number in the case of their deficiency through magnification and compensation, as has been shown for rRNA genes by other authors.

[Aminoglycoside-3'-phosphotransferase from Actinomyces fradiae. The identification of its inactivation product]. / Aminoglikozid-3'-fosfotransferaza iz Actinomyces fradiae. Identifikatsiia produkta inaktivatsii.

Neomycin phosphate was obtained as a result of neomycin phosphorylation with aminoglycoside-phosphotransferase from Act. fradiae. It was isolated from the reaction mixture and purified. Successive ion exchange chromatography on columns with Amberlite IRC-50 (NH+4 form), Dowex 1 X 10 (OH- form) and Amberlite CG-50 (NH+4 form) was used for purification of the inactivation product. The findings of the elementary analysis of neomycin phosphate showed the presence of 1 mole of phosphorus per 1 mole of the antibiotic. From the results of the chemical analysis, IR- and NMR-spectrometry neomycin phosphate and neamine phosphate obtained from it by methanolysis were identified as neomycin-3'-phosphate and neamine-3'-phosphate, respectively. The data indicate that the enzyme isolated from Act. fradiae is aminoglycoside-3'-phosphotransferase.

[Aminoglycoside-3'-phosphotransferase I from aminoglycoside-polyresistant strain E. coli 182]. / Aminoglikozid-3'-fosfotransferaza I iz kletok E. Coli 182 s mnozhestvennoi ustoichivost'iu k aminoglikozidnym antibiotikam.

An aminoglycoside-3'-phosphotransferase I catalyzing phosphorylation of some aminoglycoside antibiotics with the 3'-hydroxyl group has been purified from the cells of aminoglycoside resistant strain E. coli 182 by competitive affinity chromatography on neomycin-Sepharose and gel-filtration on Sephadex G-100. The product of enzymatic phosphorylation of kanamycin A was isolated and identified as kanamycin-3'-phosphate by NMR, thin-layer chromatography and chemical characterization. The kinetic properties of the enzyme were studied. The pH-optimum was between 7,8--8,0; the [S]0.5 values for kanamycin, neomycin and paromomycin were 2.10(-5) M, the energy of activation was 15,9 kcal/mol. The bivalent cations were required for activity of the enzyme, Mg2+ was the most effecient. The relative aminoglycoside antibiotics containing no 3'-hydroxyl group were competitive inhibitors of the enzyme activity with Ki values close to [S]0.5.