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Wyświetlanie 1-10 z 20
Tytuł:
Location of markers of aluminium tolerance genes on rye chromosomes (Secale cereale L.)
Autorzy:
Wiśniewska, Iwona
Rafalski, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/2199029.pdf
Data publikacji:
2006-06-22
Wydawca:
Instytut Hodowli i Aklimatyzacji Roślin
Tematy:
aluminium tolerance
chromosomal location
DNA-DNA hybridisation
PCR markers
wheat/rye addition lines
Opis:
The aim of presented work was to identify of PCR amplifiedDNAfragments differentiating aluminium tolerant and sensitive forms of rye and to locate the markers on rye chromosomes. For identification of markers, the PCR system with semi-specific primers targeting intron-exon sequences of plant genes was applied. The modified method of bulked segregant analysis was used. The pooled DNAs of two or three F2 segregating populations were screened together with DNA of their parental inbred lines. Potential marker of tolerance gene was located on rye chromosomes using wheat/rye (Chinese Spring/Blanco) additional lines. The specific probes obtained from DNA fragments differentiating sensitive and tolerant forms of rye were hybridized to PCR amplified DNA fragments of sensitive and tolerant forms of rye and the set of wheat/rye addition lines. Independently of the method of digoxygenin labelling (primer extension or Taq polymerase reaction), the probes obtained showed similar hybridization patterns. The results of hybridisation of 21 probes prepared from 12 DNA fragments confirmed connection of selected DNA fragments with to aluminium tolerance or sensitivity. Most of these DNA fragments originated from tolerant forms of rye. Using this method it was possible to locate eight DNA fragments on rye chromosomes. Three DNA fragments hybridised to chromosome 4R, two DNA fragments to chromosome 6R and single DNA fragments to chromosomes 1R, 2R and 3R. Four DNA fragments indicating clear relationship with character studied were not located on particular chromosomes using this set of wheat/rye addition lines. Hybridisation of probes prepared from four DNA fragments revealed length polymorphism. Probes prepared from two DNA fragments were characterised as dominant markers. In other cases the type of marker (dominant/codominat) was not fully documented.
Źródło:
Plant Breeding and Seed Science; 2006, 53; 43-52
1429-3862
2083-599X
Pojawia się w:
Plant Breeding and Seed Science
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Integracja euroazjatycka : rosyjska próba ekonomicznego scalenia obszaru poradzieckiego
Autorzy:
Wiśniewska, Iwona.
Fischer, Ewa.
Współwytwórcy:
Ośrodek Studiów Wschodnich im. Marka Karpia ; Warszawa
Data publikacji:
2013
Wydawca:
Warszawa : Ośr. Studiów Wschodnich im. Marka Karpia
Tematy:
Integracja gospodarcza
Polityka
Opis:
Współwyd. w kierunku przeciwnym: Eurasian integration : Russia's attempt at the economic unification of the post-soviet area / Iwona Wiśniewska ; coop. Ewa Fisher [et al.].
Dostawca treści:
Bibliografia CBW
Książka
Tytuł:
Molecular probes for detection of wheat chromosomal fragments in rye.
Autorzy:
Rafalski, Andrzej
Wiśniewska, Iwona
Sikora, Teresa
Łapiński, Bogusław
Powiązania:
https://bibliotekanauki.pl/articles/2198780.pdf
Data publikacji:
2000-12-20
Wydawca:
Instytut Hodowli i Aklimatyzacji Roślin
Tematy:
introgression
PCR
rye
Southern blotting
Triticum durum probe
wheat
wheat specific probes
Opis:
Twelve DNA fragments amplified on templates of Triticum urartu, Aegilops speltoides and Aegilops squarrosa were separated, reamplified and used as digoxigenin-labelled probes. The species and genome specificity of probes was evaluated by Southern dot-blot hybridisation to Triticum durum, the donors of wheat genomes, rye and rye with introgressed wheat chromosome fragments. In comparison to labelled genomic DNA of T. durum, the probes obtained by labelling PCR-amplified fragments exhibited higher specificity to wheat genomes. Under the applied hybridisation conditions all probes showed different degree of cross-hybridisation to rye DNA. Some probes indicated quantitative difference in their specificity to wheat genomes, but generally the intensity of hybridisation to the genomes A, S and D was independent of the origin of an amplified fragment. Selected probes, used in dot-blot hybridisation system together with genomic DNA of T. durum, may increase the sensitivity of screening wheat chromosomal fragments introgressed to rye.
Źródło:
Plant Breeding and Seed Science; 2000, 44; 27-37
1429-3862
2083-599X
Pojawia się w:
Plant Breeding and Seed Science
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Wyspa na uwięzi : Kaliningrad między Moskwą a UE
Autorzy:
Rogoża, Jagoda.
Wierzbowska-Miazga, Agata.
Wiśniewska, Iwona (1975- ).
Współwytwórcy:
Duchnowicz, Ilona. Tłumaczenie
Todd, Jim. Tłumaczenie
Data publikacji:
2012
Wydawca:
Warszawa : Ośrodek Studiów Wschodnich im. Marka Karpia
Tematy:
Unia Europejska (UE)
Polityka
Opis:
Współwyd. w kierunku przeciwnym: A captive island : Kaliningrad between Moscow and the EU / Jadwiga Rogoża, Agata Wierzbowska-Miazga, Iwona Wiśniewska ; [transl. Ilona Duchnowicz, coop. Jim Todd].
Dostawca treści:
Bibliografia CBW
Książka
Tytuł:
Influence of the Electrolyte Type on the Adsorption and Electrokinetic Properties of the Ionic Polyamino Acids – Cr2O3 system
Autorzy:
Ostolska, Iwona
Wiśniewska, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/951402.pdf
Data publikacji:
2013
Wydawca:
Uniwersytet Marii Curie-Skłodowskiej. Wydawnictwo Uniwersytetu Marii Curie-Skłodowskiej
Tematy:
Polyamino acid
polyaspartic acid
polylysine
chromium (III) oxide
polymer adsorption
potentiometric titration
zeta potential
Opis:
The influence of a kind of support electrolyte on the ionic polyamino acids adsorption at the chromium (III) oxide – polymer solution interface was investigated. The NaCl and CaCl2 were used as the background electrolytes. In order to determine the effect of the electrolyte, the same value of ionic strength of the test solutions were taken. It was proved that formation of intermolecular and intramolecular complexes in the presence of divalent calcium ions is responsible for essential changes in polymer adsorption. Related to the ionic character of polyamino acid two different adsorption behaviours can be observed. The increase of the ASP adsorption amount in the presence of calcium ions may be explained by formation of complexes between the dissociated carboxylic groups and Ca2+ ions. The opposite situation takes place in the case of polylysine – the application of CaCl2 results in the dramatic decrease in the polymer adsorption caused by blocking the active sites available for LYS macromolecules. In order to make a comprehensive analysis, the zeta potential and surface charge density measurements were performed taking into account the kind of the background electrolyte. The above-mentioned tests were carried out in the absence and presence of the polyamino acid at two different concentrations – 10 and 100 ppm respectively.
Źródło:
Annales Universitatis Mariae Curie-Skłodowska, sectio AA – Chemia; 2013, 68, 1-2
2083-358X
Pojawia się w:
Annales Universitatis Mariae Curie-Skłodowska, sectio AA – Chemia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Role of oligochitosans in regulation of cellular activity and location of pyruvate kinase (pk) isoenzyme m2 that affects proliferation of ehrlich ascites tumor cells (eat)
Autorzy:
Ignacak, Jan
Wiśniewska-Wrona, Maria
Pałka, Iwona
Niekraszewicz, Antoni
Powiązania:
https://bibliotekanauki.pl/articles/1035231.pdf
Data publikacji:
2013
Wydawca:
Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
Tematy:
isoenzyme M1 and M2 pyruvate kinase
nucleus
oligochitosans
ε-methyl-L-lysyne
Opis:
The pyruvate kinase isoenzyme M2 originating from the nucleoplasm and cytoplasm of tumor cells, with its highest affinity to the 2-phosphoenolpyruvate (2-PEP) and sensitivity to L-cysteine, contributes to an increased generation of energy as ATP, necessary for tumor cell proliferation. In the presence of L-cysteine, the isoenzyme M2 PK demonstrates the activity of histone kinase, transferring the phosphoryl group from 2-PEP to the ε-amine residue of the H1 histone lysine. Oligochitosans induce expression of the inducible nitric oxide synthase gene (iNOS), what results in an increased synthesis of nitric oxide, which reacts with L-cysteine and produces L-S-nitrosocysteine. Lack of L-cysteine contributes to inhibition of kinase activity of the H1 histone, an M2 PK isoenzyme. Decreased phosphorylation of the H1 histone contributes to inhibition of EAT cell proliferation. No effect on proliferation of normal cells that include the PK M1 isoenzyme has been observed in the presence of oligochitosans.
Źródło:
Progress on Chemistry and Application of Chitin and its Derivatives; 2013, 18, 18; 67-76
1896-5644
Pojawia się w:
Progress on Chemistry and Application of Chitin and its Derivatives
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Role of oligochitosans in regulation of cellular activity and location of pyruvate kinase (pk) isoenzyme m2 that affects proliferation of ehrlich ascites tumor cells (eat)
Autorzy:
Ignacak, Jan
Wiśniewska-Wrona, Maria
Pałka, Iwona
Niekraszewicz, Antoni
Powiązania:
https://bibliotekanauki.pl/articles/1035209.pdf
Data publikacji:
2013
Wydawca:
Sieć Badawcza Łukasiewicz - Polskie Towarzystwo Chitynowe
Tematy:
isoenzyme M1 and M2 pyruvate kinase
nucleus
oligochitosans
ε-methyl-L-lysyne
Opis:
The pyruvate kinase isoenzyme M2 originating from the nucleoplasm and cytoplasm of tumor cells, with its highest affinity to the 2-phosphoenolpyruvate (2-PEP) and sensitivity to L-cysteine, contributes to an increased generation of energy as ATP, necessary for tumor cell proliferation. In the presence of L-cysteine, the isoenzyme M2 PK demonstrates the activity of histone kinase, transferring the phosphoryl group from 2-PEP to the ε-amine residue of the H1 histone lysine. Oligochitosans induce expression of the inducible nitric oxide synthase gene (iNOS), what results in an increased synthesis of nitric oxide, which reacts with L-cysteine and produces L-S-nitrosocysteine. Lack of L-cysteine contributes to inhibition of kinase activity of the H1 histone, an M2 PK isoenzyme. Decreased phosphorylation of the H1 histone contributes to inhibition of EAT cell proliferation. No effect on proliferation of normal cells that include the PK M1 isoenzyme has been observed in the presence of oligochitosans.
Źródło:
Progress on Chemistry and Application of Chitin and its Derivatives; 2013, 18, 18; 67-76
1896-5644
Pojawia się w:
Progress on Chemistry and Application of Chitin and its Derivatives
Dostawca treści:
Biblioteka Nauki
Artykuł
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