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    Wyświetlanie 1-3 z 3
    Tytuł:
    Contents of total and protein-bound carbohydrates are low in leukemic leukocytes from patients with acute myelogenous leukemia
    Autorzy:
    Smoleńska-Sym, Gabriela
    Zdebska, Ewa
    Gołaszewska, Ewa
    Woźniak, Jolanta
    Durżyński, Tomasz
    Maj, Stanisław
    Mokras, Urszula
    Kościelak, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044811.pdf
    Data publikacji:
    1998
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Źródło:
    Acta Biochimica Polonica; 1998, 45, 2; 361-371
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The activity of cathepsin D and alpha-1 antitrypsin in hip and knee osteoarthritis
    Autorzy:
    Olszewska-Slonina, Dorota
    Matewski, Dariusz
    Jung, Stanislaw
    Olszewski, Krzysztof
    Czajkowski, Rafal
    Braszkiewicz, Joanna
    Wozniak, Alina
    Kowaliszyn, Bogna
    Powiązania:
    https://bibliotekanauki.pl/articles/1039618.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protease
    cathepsin D
    alpha 1-antitrypsin
    antiprotease
    cartilage
    osteoarthritis
    Opis:
    The progress of cartilage decay during joint degeneration is not well monitored with biochemical methods. The role of cathepsin D (CAT-D) in articular cartilage deterioration remains unclear. The aim of this study is to assess the activity of CAT-D and alpha-1 antitrypsin (AAT) in blood in patients with hip or knee osteoarthritis. The activity of CAT-D and AAT in blood serum of 40 women and 21 men with hip or knee osteoarthritis was determined before total joint replacement, on the tenth day after surgery, and once in 54 healthy patients. The preoperative activity of CAT-D in patients with osteoarthritis was lower by 53.6% (11.00 ± 4.54 10-2 nM released tyrosine/mg protein/min, P < 0.001) and after surgery by 55.0% (10.67 ± 4.64 10-2 nM released tyrosine/mg protein/min, P < 0.001) when compared to its activity in healthy patients. There was no significant statistical difference between CAT-D activity before the surgery and its activity on the tenth day after it in the analyzed group (P< 0.496). Simultaneously, the preoperative activity of AAT in the OA (osteoarthritis) patients was by 25.5% (0.93 ± 0.32 mg inhibited trypsin/ml blood serum, P < 0.001) and postoperative was by 44.9% higher (1.26 ± 0.36 mg inhibited trypsin/ml blood serum, P < 0.001) than in healthy patients. The low CAT-D activity in osteoarthritis of big joints is associated with a decrease of cartilage cells during the degenerative process. The higher activity of acute phase protein AAT in OA patients' blood serum confirms the inflammatory component in the osteoarthritis process.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 1; 99-106
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Theoretical models of catalytic domains of protein phosphatases 1 and 2A with Zn2+ and Mn2+ metal dications and putative bioligands in their catalytic centers.
    Autorzy:
    Woźniak-Celmer, Edyta
    Ołdziej, Stanisław
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044161.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphatase inhibitors
    constrained simulated annealing
    protein phosphatase 1A and 2B
    molecular dynamics
    homology modeling
    Opis:
    The oligomeric metalloenzymes protein phosphatases dephosphorylate OH groups of Ser/Thr or Tyr residues of proteins whose actions depend on the phosphorus signal. The catalytic units of Ser/Thr protein phosphatases 1, 2A and 2B (PP1c, PP2Ac and PP2Bc, respectively), which exhibit about 45% sequence similarity, have their active centers practically identical. This feature strongly suggests that the unknown structure of PP2Ac could be successfully homology-modeled from the known structures of PP1c and/or PP2Bc. Initially, a theoretical model of PP1c was built, including a phosphate and a metal dication in its catalytic site. The latter was modeled, together with a structural hydroxyl anion, as a triangular pseudo-molecule (Zno or Mno), composed of two metal cations (double Zn2+ or Mn2+, respectively) and the OH- group. To the free PP1c two inhibitor sequences R29RRRPpTPAMLFR40 of DARPP-32 and R30RRRPpTPATLVLT42 of Inhibitor-1, and two putative substrate sequences LRRApSVA and QRRQRKpRRTI were subsequently docked. In the next step, a free PP2Ac model was built via homology re-modeling of the PP1c template and the same four sequences were docked to it. Thus, together, 20 starting model complexes were built, allowing for combination of the Zno and Mno pseudo-molecules, free enzymes and the peptide ligands docked in the catalytic sites of PP1c and PP2Ac. All models were subsequently subjected to 250-300 ps molecular dynamics using the AMBER 5.0 program. The equilibrated trajectories of the final 50 ps were taken for further analyses. The theoretical models of PP1c complexes, irrespective of the dication type, exhibited increased mobilities in the following residue ranges: 195-200, 273-278, 287-209 for the inhibitor sequences and 21-25, 194-200, 222-227, 261, 299-302 for the substrate sequences. Paradoxically, the analogous PP2Ac models appeared much more stable in similar simulations, since only their "prosegment" residues 6-10 and 14-18 exhibited an increased mobility in the inhibitor complexes while no areas of increased mobility were found in the substrate complexes. Another general observation was that the complexes with Mn dications were more stable than those with Zn dications for both PP1c and PP2Ac units.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 35-52
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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