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    Wyświetlanie 1-6 z 6
    Tytuł:
    Prognostic role of clinical presentation, cytological picture and response to treatment in canine centroblastic lymphoma
    Autorzy:
    Kliczkowska-Klarowicz, K.
    Jagielski, D.
    Czopowicz, M.
    Sapierzyński, R.
    Powiązania:
    https://bibliotekanauki.pl/articles/2087233.pdf
    Data publikacji:
    2021
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    lymphoma
    prognostic factors
    chemotherapy
    asparaginase
    mitoxantron
    Źródło:
    Polish Journal of Veterinary Sciences; 2021, 24, 1; 101-107
    1505-1773
    Pojawia się w:
    Polish Journal of Veterinary Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structural aspects of l-asparaginases, their friends and relations
    Autorzy:
    Michalska, Karolina
    Jaskolski, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1041150.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ntn-hydrolase
    l-asparaginase
    isoaspartyl peptidase
    Opis:
    Enzymes capable of converting l-asparagine to l-aspartate can be classified as bacterial-type or plant-type l-asparaginases. Bacterial-type l-asparaginases are further divided into subtypes I and II, defined by their intra-/extra-cellular localization, substrate affinity, and oligomeric form. Plant-type l-asparaginases are evolutionarily and structurally distinct from the bacterial-type enzymes. They function as potassium-dependent or -independent Ntn-hydrolases, similar to the well characterized aspartylglucosaminidases with (αβ)2 oligomeric structure. The review discusses the structural aspects of both types of l-asparaginases and highlights some peculiarities of their catalytic mechanisms. The bacterial-type enzymes are believed to have a disordered active site which gets properly organized on substrate binding. The plant-type enzymes, which are more active as isoaspartyl aminopeptidases, pose a chemical challenge common to other Ntn-hydrolases, which is how an N-terminal nucleophile can activate itself or cleave its own α-amide bond before the activation is even possible. The K+-independent plant-type l-asparaginases show an unusual sodium coordination by main-chain carbonyl groups and have a key arginine residue which by sensing the arrangement at the oligomeric (αβ)-(αβ) interface is able to discriminate among substrates presented for hydrolysis.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 4; 627-640
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    A comparison between the crystal and solution structures of Escherichia coli asparaginase II.
    Autorzy:
    Kozak, Maciej
    Jurga, Stefan
    Powiązania:
    https://bibliotekanauki.pl/articles/1043790.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    structure in solution
    small angle X-ray scattering
    asparaginase
    Opis:
    The small angle X-ray scattering (SAXS) pattern of the homotetrameric asparaginase II from Escherichia coli was measured in solution in conditions resembling those in which its crystal form was obtained and compared with that calculated from the crystallographic model. The radius of gyration measured by SAXS is about 5% larger and the maximum dimension in the distance distribution function about 12% larger than the corresponding value calculated from the crystal structure. A comparison of the experimental and calculated distance distribution functions suggests that the overall quaternary structure in the crystal and in solution are similar but that the homotetramer is less compact in solution than in the crystal.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 509-513
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Sequence analysis of enzymes with asparaginase activity.
    Autorzy:
    Borek, Dominika
    Jaskólski, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1044033.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    N-terminal nucleophile hydrolase
    lysophospholipase
    tRNA amidotransferase
    aspartylglucosaminidase
    asparaginase
    L-asparagine
    Opis:
    Asparaginases catalyze the hydrolysis of asparagine to aspartic acid and ammonia. Enzymes with asparaginase activity play an important role both in the metabolism of all living organisms as well as in pharmacology. The main goal of this paper is to attempt a classification of all known enzymes with asparaginase activity, based on their amino acid sequences. Some possible phylogenetic consequences are also discussed using dendrograms and structural information derived from crystallographic studies.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 893-902
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    L-asparaginase: An ultimate anti-neoplastic enzyme
    Autorzy:
    Prasad Talluri, V.S.S.L.
    Bhavana, M.
    Mahesh Kumar, M.V.S.
    Rajagopal, S.V.
    Powiązania:
    https://bibliotekanauki.pl/articles/11250.pdf
    Data publikacji:
    2014
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    L-asparaginase
    anti-neoplastic enzyme
    enzyme
    acute lymphoblastic leukemia
    chemotherapeutic drug
    Opis:
    The objective of the study described the importance of L-asparaginase and its importance in the field of medicine. Different types of enzymes are produced based on the adaptation to the environment where the living organisms live to tune the metabolic pathways according to their adapted changes. The enzymes present in various organs are produced by many cell types in multicellular organisms. Except ribosomes all other known enzymes are proteinaceous in nature. L-asparaginase is a potential therapeutic agent for acute lymphoblastic leukemia (ALL) and chronic myelogenous leukemia which is approved by FDA & WHO. L-asparaginase catalyzes the deamination of L-asparagine to L-aspartic acid & ammonia. Unlike normal cells, malignant cells require large amount of L-asparagine for protein synthesis and cell division. From this background the present review is an effort to gather the information on the mechanism, sources, molecular details and application of L-asparaginase enzyme.
    Źródło:
    International Letters of Natural Sciences; 2014, 10
    2300-9675
    Pojawia się w:
    International Letters of Natural Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Characterisation and molecular dynamic simulations of J15 asparaginase from Photobacterium sp. strain J15
    Autorzy:
    Yaacob, Mohd
    Hasan, Wan
    Ali, Mohd
    Rahman, Raja
    Salleh, Abu
    Basri, Mahiran
    Leow, Thean
    Powiązania:
    https://bibliotekanauki.pl/articles/1039206.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    J15 asparaginase
    Photobacterium sp.
    expression
    purification
    Molecular Dynamic (MD) simulations
    Opis:
    Genome mining revealed a 1011 nucleotide-long fragment encoding a type I l-asparaginase (J15 asparaginase) from the halo-tolerant Photobacterium sp. strain J15. The gene was overexpressed in pET-32b (+) vector in E. coli strain Rosetta-gami B (DE3) pLysS and purified using two-step chromatographic methods: Ni2+-Sepharose affinity chromatography and Q-Sepharose anion exchange chromatography. The final specific activity and yield of the enzyme achieved from these steps were 20 U/mg and 49.2%, respectively. The functional dimeric form of J15-asparaginase was characterised with a molecular weight of ~70 kDa. The optimum temperature and pH were 25°C and pH 7.0, respectively. This protein was stable in the presence of 1 mM Ni2+ and Mg2+, but it was inhibited by Mn2+, Fe3+ and Zn2+ at the same concentration. J15 asparaginase actively hydrolysed its native substrate, l-asparagine, but had low activity towards l-glutamine. The melting temperature of J15 asparaginase was ~51°C, which was determined using denatured protein analysis of CD spectra. The Km, Kcat, Kcat/Km of J15 asparaginase were 0.76 mM, 3.2 s-1, and 4.21 s-1 mM-1, respectively. Conformational changes of the J15 asparaginase 3D structure at different temperatures (25°C, 45°C, and 65°C) were analysed using Molecular Dynamic simulations. From the analysis, residues Tyr24, His22, Gly23, Val25 and Pro26 may be directly involved in the 'open' and 'closed' lid-loop conformation, facilitating the conversion of substrates during enzymatic reactions. The properties of J15 asparaginase, which can work at physiological pH and has low glutaminase activity, suggest that this could be a good candidate for reducing toxic effects during cancer treatment.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 4; 745-752
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-6 z 6

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