Wyniki wyszukiwania - Biblioteka Nauki

1

Metody rzadkiego ciecia DNA

100%

Kur J.

Postępy Mikrobiologii

|

1992

|

tom 31

|

nr 3-4

225-234

2

Integration host factor [IHF] applied for partial digestion by restriction endonucleases in large DNA molecules [IARC procedure]

100%

Kur J.

|

1993

|

tom 42

|

nr 2

3

Plejotropowy charakter histonopodobnego bialka Escherichia coli - IHF

88%

Kur J.

Postępy Mikrobiologii

|

1992

|

tom 31

|

nr 3-4

235-256

4

Molecular biotechnology - a new era in biotechnology

75%

Kur J.

|

nr 3A

747

5

Identyfikacja i izolacja genu kodującego zaadaptowana do zimna B-galaktozydazę Paracoccus sp.

63%

Wierzbicka A. , Kur J.

|

2009

|

tom 16

6

Nurkowanie badawcze w naukach przyrodniczych

63%

Kur J. , Mioduchowska M.

Polish Hyperbaric Research

|

2018

|

tom nr 4(65)

55--62

PL

Nurkowanie w celach naukowych, z wykorzystaniem odpowiedniego sprzętu w postaci aparatów oddechowych, jest coraz częściej wykorzystywane do licznych badań. Co więcej, taka forma nurkowania pozwala na prowadzenie badań interdyscyplinarnych. Aktualna nomenklatura ten rodzaj nurkowania definiuje jako nurkowanie w celu zbierania informacji, służących szeroko pojętej nauce lub wspieranie idei nauki wykorzystując techniki nurkowania. Technika badań podwodnych jest szczególnie istotna w naukach przyrodniczych, gdzie umożliwia nieinwazyjne obserwacje fauny i flory ekosystemów wodnych w ich naturalnym środowisku. Jednocześnie zastosowanie nurkowania w celach naukowych pozwala uniknąć błędów, popełnianych przy losowym pobieraniu materiału, co związane jest ze stosowaniem klasycznej metodyki próbkowania. W rezultacie takie nurkowanie ma kluczowe znaczenie w analizach systematycznych, ekologicznych czy behawioralnych. Niemniej jednak technika nurkowania, jakkolwiek uniwersalna, wymaga optymalizacji, odrębnych opracowań i usystematyzowania, zależnie od rodzaju prowadzonych badań naukowych. Niniejsza praca umożliwia poznanie znaczenia nurkowania prowadzonego w celach naukowych oraz systematyzuje podstawowe pojęcia związane z zasadami regulacji prawnych w Polsce jak i za granicami kraju.

EN

Scientific diving is increasingly being used for numerous studies. Moreover, this form of diving allows for the conduction of interdisciplinary research. The current nomenclature of this type of dive is defined as scuba diving to collect information to support science by using diving techniques. Underwater research is particularly important in the natural sciences where it allows for the non-invasive observations of fauna and flora of aquatic ecosystems in their natural environment. At the same time, the use of diving for scientific purposes avoids mistakes made in random sampling, which is related to the use of classical sampling methods. As a result, such diving is crucial in systematic, ecological and behavioural analysis. Nevertheless, dive techniques, however versatile, require optimisation, separate study and systematisation, depending on the type of research conducted. This article is an attempt to present an outline of the topic, to systematise basic concepts in presenting the principles of legal regulations in Poland and abroad.

7

Techniki biologii molekularnej w analityce produktow przemyslu miesnego

63%

Szweda P. , Kur J.

|

2005

|

nr 08-09

54

8

Beta-D-galaktozydazy - zrodla, wlasciwosci i zastosowanie

63%

Wanarska M. , Kur J.

Biotechnologia

|

2005

|

nr 4

46-62

9

Recombinant His-tagged DNA polymerase. II. Cloning and purification of Thermus aquaticus recombinant DNA polymerase [Stoffel fragment]

63%

Dabrowski S. , Kur J.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

EN

The Stoffel DNA fragment, shortened by 12 bp from 5' end, coding for StoffelDNA polymerase (missing 4 amino acids at N-terminus of Stoffel amino-acids sequence) from the thermophilic Thermus aquaticus (strain YT-1) was amplified, cloned and expressed in Escherichia coli. The recombinant Stoffel fragment contained a polyhistidine tag at the N-terminus (21 additional amino acids) that allowed its single-step isolation by Ni2+ affinity chromatography. The enzyme was characterized and displayed high DNA polymerase activity and thermostability evidently higher than the native Tag DNA polymerase.

10

Binding of Escherichia coli integration host factor [IHF] to the origin segment of p15A plasmid

63%

Hiszczynska-Sawicka E. , Kur J.

|

nr 1

EN

The integration host factor (IHF) is a sequence-specific, histone-like, multi-fun- ctional DNA-binding and -bending protein of Escherichia coli. Characterization and functional analysis of this protein has been carried out mainly in bacteriophage λ and other mobile genetic elements. In this paper we report data concerning the binding of IHF protein to the plasmid oripl5A region. IHF binds to the single site of the DNA fragment containing the oripl5A, as shown by the gel mobility shift assays and footprinting experiment. On the basis of the ihf consensus sequences published, we have been able to identify one sequence of putative ihf site into the oripl5A sequence with two mismatches in relation to the consensus sequence of Kur et al., 1989, Gene 81,1-15. One ihf binding site was also found in the oriColEl region sequence with three mismatches in relation to this consensus sequence.

11

Recombinant His-tagged DNA polymerase. I. Cloning, purification and partial characterization of Thermus thermophilus recombinant DNA polymerase

63%

Dabrowski S. , Kur J.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

EN

The Tth DNA polymerase gene from the thermophilic Thermus thermophilus (strain HB8) was amplified, cloned and expressed in Escherichia coli. The recombinant DNA polymerase containing a polyhistidine tag at the N-terminus was isolated in a single step by Ni2+ affinity chromatography. The purified recombinant enzyme, showing high polymerase activity contained 43 additional amino-acid residues (including a cluster of six histidine residues inserted for purification of the recombinant protein by metal-affinity chromatography) at N-terminus. The applied overexpression system was very efficient giving 700000 u of DNA polymerase activity from 1 liter of induced culture. The enzyme was characterized and displayed high DNA polymerase and reverse transcriptase activities and high thermostability as compared to the native Tht DNA polymerase.

12

Purification of IHF-like protein from gram-negative bacteria in one chromatographic step

63%

Krawczyk B. , Kur J.

|

tom 43

|

nr 2

EN

We describe a fast and very efficient method of purification which yields highly purified integration host factor-like proteins in one chromatografie step. IHF-like proteins from Acinetobacter junii or Proteus vulgaris are each an a£ heterodimer (subunits of 10 and 11 kDa) similar to the IHF of Escherichia coli when analyzed by polyacrylamide gel electrophoresis. The purified IHF are able to bind to the same ihf sites as IHF of E. coli. The results presented confirm that IHF is conserved during evolution in gram-negative bacteria.

13

A new PCR system for Agrobacterium tumefaciens detection based on amplification of T-DNA fragment

63%

Sachadyn P. , Kur J.

|

nr 2

14

PCR systems for Agrobacterium tumefaciens detection

63%

Sachadyn P. , Kur J.

|

nr 2

15

Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins [SSB]

63%

Filipkowski P. , Kur J.

|

tom 54

|

nr 1

EN

To study the biochemical properties of SSB's from Deinococcus grandis (DgrSSB) and Deinococcus proteolyticus (DprSSB), we have cloned the ssb genes obtained by PCR and have developed Escherichia coli overexpression systems. The genes consist of an open reading frame of 891 (DgrSSB) and 876 (DprSSB) nucleotides encoding proteins of 296 and 291 amino acids with a calculated molecular mass of 32.29 and 31.33 kDa, respectively. The amino-acid sequence of DgrSSB exhibits 45%, 44% and 82% identity and the amino-acid sequence of DprSSB reveals 43%, 43% and 69% identity with Thermus aquaticus (TaqSSB), Thermus thermophilus (TthSSB) and Deinococcus radiodurans SSBs, respectively. We show that DgrSSB and DprSSB are similar to Thermus/Deinococcus SSBs in their biochemical properties. They are functional as homodimers, with each monomer encoding two single-stranded DNA binding domains (OB-folds). In fluorescence titrations with poly(dT), both proteins bind single-stranded DNA with a binding site size of about 33 nt per homodimer. In a complementation assay in E. coli, DgrSSB and DprSSB took over the in vivo function of EcoSSB. Thermostability with half-lives of about 1 min at 65-67.5°C make DgrSSB and DprSSB similar to the known SSB of Deinococcus radiodurans (DraSSB).

16

Integration host factor, a histone - like Escherichia coli protein, binds to at least four sites of the DNA fragment containing the recA gene

63%

Krawczyk B. , Kur J.

Acta Microbiologica Polonica

|

1994

|

tom 43

|

nr 2

17

The construction of beta-galactosidase-muts fusion protein

51%

Zielinska A. , Stanislawska A. , Sachadyn P. , Kur J.

|

nr 3A

770

18

Production and purification of recombinant His-tag-aqualysin I of Thermus aquaticus by Escherichia coli

51%

Sobiewska-Oledzka G. , Dabrowski S. , Kur J.

|

nr 3A

767

19

Epidemiological study of Toxoplasma gondii infection among cattle in Northern Poland

51%

Holec-Gasior L. , Drapala D. , Dominiak-Gorski B. , Kur J.

|

2013

|

tom 20

|

nr 4

20

Zastosowanie metody PCR do wykrywania Listeria monocytogenes w mleku

51%

Wieckowska M. , Kotlowski R. , Kur J. , Rudnicka W.

Medycyna Doświadczalna i Mikrobiologia

|

1998

|

tom 50

|

nr 3-4

251-257

PL

Przeprowadzono elektroforetyczne i serologiczne badania porównawcze składu białek 6 szczepów M. pneumoniae i 1 szczepu M. genitalium. Stwierdzono pełne podobieństwo budowy antygenowej badanych szczepów M. pneumoniae oraz bliskie podobieństwo antygenowe M. genitalium do M. pneumoniae. Najbardziej swoistymi spośród antygenów M. pneumoniae okazały się białka o masie cząsteczkowej 170 (białko P1) i 89 kDa, uważane za najważniejsze adhezyny komórki mykoplazmowej.

EN

The Mycoplasma pneumoniae FH strain routinely used in our laboratory for over 25 years as antigen in serological tests, 2 reference M. pneumoniae strains from ATCC (29342 and M129) and 3 isolates of M. pneumoniae obtained in 1995 from pneumonia patients were compared by SDS-PAGE, complement fixation test (CFT) and by Western-immunoblotting against human and rabbit serum samples with high level of mycoplasmal antibodies. On SDS-PAGE all M. pneumoniae strains showed the same number of 23 polypeptides on the gel with identical molecular weights. The same strains on immunoblotting against human and rabbit serum samples showed six bands: 170, 89, 75, 55, 38 and 33 kDa with the strongest antibody staining in 170-(P1 protein) and 89-kDa bands. Because of its known antigenic relationships Mycoplasma genitalium was used for comparison. The pattern of M genitalium proteins on SDS-PAGE was similar to pattern of M. pneumoniae but distinguishable. On immunoblotting six proteins of M. genitalium (135, 127, 110, 95, 75 and 45 kDa) reacted with human and rabbits immunoglobulins for M. pneumoniae antigens. Furthermore in complement fixation test both antigens, prepared from M. pneumoniae and M. genitalium, reacted as well with human and rabbit immunoglobulins for M. pneumoniae and with rabbit immunoglobulins for M. genitalium. These cross-reactions observed in serological techniques could give false positive results in routine diagnosis of M. pneumoniae infections. In such situations showing on immunoblott of presence in tested serum sample of antibodies to 170 - and 89 kDa proteins could confirm M. pneumoniae infection.