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Wyszukujesz frazę "protein phosphatase" wg kryterium: Temat


Wyświetlanie 1-13 z 13
Tytuł:
The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity.
Autorzy:
Szalewicz, Agata
Strzelczyk, Barbara
Sopel, Mirosław
Kubicz, Aleksandra
Powiązania:
https://bibliotekanauki.pl/articles/1043638.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
metallophosphatase
acid phosphatase
frog liver
protein phosphatase
tyrosine protein phosphatase
Opis:
The cellular localization of the 35 kDa, low molecular mass acid metallophosphatase (LMW AcPase) from the frog (Rana esculenta) liver and its activity towards P-Ser and P-Tyr phosphorylated peptides were studied. This enzyme was localized to the cytoplasm of hepatocytes but did not appear in other cells of liver tissue (endothelium, macrophages, blood cells). This LMW AcPase does not display activity towards 32P-phosphorylase a under conditions standard for the enzymes of PPP family. Proteins containing P-Ser: rabbit 32P-phosphorylase a and phosvitin are hydrolysed only at acidic pH and are poor substrates for this enzyme. The frog AcPase is not inhibited by okadaic acid and F- ions, the Ser/Thr protein phosphatase inhibitors. Moreover, the frog enzyme does not cross-react with specific antisera directed against N-terminal fragment of human PP2A and C-terminal conserved fragment of the eukaryotic PP2A catalytic subunits. These results exclude LMW AcPase from belonging to Ser/Thr protein phosphatases: PP1c or PP2Ac. In addition to P-Tyr, this enzyme hydrolyses efficiently at acidic pH P-Tyr phosphorylated peptides (hirudin and gastrin fragments). Km value for the hirudin fragment (7.55 ± 1.59 × 10-6 M) is 2-3 orders of magnitude lower in comparison with other substrates tested. The enzyme is inhibited competitively by typical inhibitors of protein tyrosine phosphatases (PTPases): sodium orthovanadate, molybdate and tungstate. These results may suggest that the LMW AcPase of frog liver can act as PTPase in vivo. A different cellular localization and different response to inhibition by tetrahedral oxyanions (molybdate, vanadate and tungstate) provide further evidence that LMW AcPase of frog liver is distinct from the mammalian tartrate-resistant acid phosphatases.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 555-566
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
Tytuł:
Interaction of maize (Zea mays) protein phosphatase 2A with tubulin
Autorzy:
Awotunde, Olubunmi
Lechward, Katarzyna
Krajewska, Katarzyna
Żołnierowicz, Stanisław
Muszyńska, Grażyna
Powiązania:
https://bibliotekanauki.pl/articles/1043655.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphatase 2A
tubulin
protein-protein interaction
plant cytoskeleton organization
maize
Opis:
Immunological and biochemical evidence has been obtained for an interaction of maize protein phosphatase 2A (PP2A) holoenzyme with tubulin. Tubulin co-purifies with maize seedling PP2A. Affinity chromatography of the maize PP2A preparation on immobilized tubulin revealed two peaks of phosphorylase a phosphatase activity. In one of the peaks, the catalytic (C) and constant regulatory (A) subunits of PP2A were identified by Western blotting. The subunits (C and A) of PP2A were co-immunoprecipitated from maize seedlings homogenate by an anti-α-tubulin antibody. The interaction of plant PP2A with tubulin indicates a possible role of reversible protein phosphorylation in the dynamic structure of plant cytoskeleton.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 131-138
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protein phosphatase 2A: Variety of forms and diversity of functions
Autorzy:
Lechward, Katarzyna
Awotunde, Olubunmi
Świątek, Wojciech
Muszyńska, Grażyna
Powiązania:
https://bibliotekanauki.pl/articles/1044037.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphatase 2A
signal transduction
protein-protein interactions
reversible phosphorylation
cell cycle
carcinogenesis.
Opis:
Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine-and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A associates with regulatory proteins, termed variable subunits, in order to form trimeric holoenzymes attributed with distinct substrate specificity and targeted to different subcellular compartments. PP2Ac activity can be modulated by reversible phosphorylation on Tyr307 and methylation on C-terminal Leu309. Studies on PP2A have shown that this enzyme may be implicated in the regulation of metabolism, transcription, RNA splicing, translation, differentiation, cell cycle, oncogenic transformation and signal transduction.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 921-933
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular Cloning and Functional Characterization of Protein Phosphatase 2C of Two Scuticociliates – Uronema marinum and Miamiensis avidus (Ciliophora: Scuticociliatia)
Autorzy:
Lee, Eun Hye
Kim, Ki Hong
Powiązania:
https://bibliotekanauki.pl/articles/763417.pdf
Data publikacji:
2010
Wydawca:
Uniwersytet Jagielloński. Wydawnictwo Uniwersytetu Jagiellońskiego
Tematy:
Protein phosphatase 2C (PP2C), Scuticociliates, Uronema marinum, Miamiensis avidus
Opis:
Complementary DNAs (cDNAs) of protein phosphatase 2C (PP2C) were cloned from two marine scuticociliates Uronema marinum and Miamiensis avidus. Both PP2C proteins showed structural characteristics of typical PP2C, such as highly conserved amino acid residues predicted for binding to phosphate and metal ions, 11 conserved PP2C motifs and 10 invariant residues. The phosphatase activity of recombinantly produced U. marinum PP2C (UmPP2C) was in proportion to the PP2C protein and Mg2+ concentrations, and was not sensitive to okadaic acid, but was inhibited by sodium fluoride, EDTA or Ca2+. The expression of UmPP2C was significantly up-regulated by exposure the ciliates with PMA suggesting that UmPP2C dephosphrylates proteins phosphorylated by protein kinases as in other eukaryotes and has a regulatory function against abrupt increase of protein phosphorylation triggered by strong stimulations.
Źródło:
Acta Protozoologica; 2010, 49, 4
1689-0027
Pojawia się w:
Acta Protozoologica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase
Autorzy:
Wysocki, Paweł
Płucienniczak, Grażyna
Strzeżek, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1040544.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
phosphorylation
boar
protein tyrosine phosphatase
seminal plasma
prostatic acid phosphatase
Opis:
Boar seminal vesicle protein tyrosine acid phosphatase (PTAP) and human prostatic acid phosphatase (PAP) show high affinity for protein phosphotyrosine residues. The physico-chemical and kinetic properties of the boar and human enzymes are different. The main objective of this study was to establish the nucleotide sequence of cDNA encoding boar PTAP and compare it with that of human PAP cDNA. Also, the amino-acid sequence of boar PTAP was compared with the sequence of human PAP. PTAP was isolated from boar seminal vesicle fluid and sequenced. cDNA to boar seminal vesicle RNA was synthesized, amplified by PCR, cloned in E. coli and sequenced. The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP. The determined sequence of a 354 bp nucleotide fragment (GenBank accession number: GQ184596) showed 90% identity with the corresponding sequence of human PAP. On the basis of this sequence a 118 amino acid fragment of boar PTAP was predicted. This fragment showed 89% identity with the corresponding fragment of human PAP and had a similar hydropathy profile. The compared sequences differ in terms of their isoelectric points and amino-acid composition. This may explain the differences in substrate specificity and inhibitor resistance of boar PTAP and human PAP.
Źródło:
Acta Biochimica Polonica; 2009, 56, 3; 481-486
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Identification, phylogenetic analyses and subcellular localization of protein phosphatases 2c type (PP2Cs) in Populus trichocarpa
Autorzy:
Betlinski, B.
Vashutina, K.
Gawronski, P.
Karpinski, S.
Powiązania:
https://bibliotekanauki.pl/articles/79950.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protein phosphatase 2C
protein kinase
mitogen-activated protein kinase
subcellular localization
Populus trichocarpa
phylogenetic analysis
identification
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
PP2A phosphatase interacts with CPK kinase and regulates pathogenesis responses triggered by intracellular ROS signals
Autorzy:
Kangasjarvi, S.
Denessiouk, K.
Trotta, A.
Konert, G.
Rahikainen, M.
Li, S.
Mhamdi, A.
Noctor, G.
Powiązania:
https://bibliotekanauki.pl/articles/80995.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protein phosphatase 2A
calcium-dependent protein kinase
reactive oxygen species
organelle
protein kinase
plant immunity
Arabidopsis
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bioaccumulation of microcystins in invasive bivalves: A case study from the boreal lagoon ecosystem
Autorzy:
Paldaviciene, A.
Zaiko, A.
Mazur-Marzec, H.
Razinkovas-Baziukas, A.
Powiązania:
https://bibliotekanauki.pl/articles/47622.pdf
Data publikacji:
2015
Wydawca:
Polska Akademia Nauk. Instytut Oceanologii PAN
Tematy:
microcystin
mussel tissue
zebra mussel
bioaccumulation
bivalve
Dreissena polymorpha
brackish water
eutrophic water
Curonian Lagoon
Baltic Sea
environment condition
biomonitoring
protein phosphatase
ELISA test
Źródło:
Oceanologia; 2015, 57, 1
0078-3234
Pojawia się w:
Oceanologia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Signalling via reactive oxygen species – why and how?
Autorzy:
Bartosz, G.
Powiązania:
https://bibliotekanauki.pl/articles/79914.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
signalling
reactive oxygen species
intracellular signalling
extracellular signalling
microorganism
animal
plant
hydrogen peroxide
protein tyrosine phosphatase
NADPH oxidase
cell wall
peroxidase
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Kinetic intermediates of unfolding of dimeric prostatic phosphatase
Autorzy:
Kuciel, Radosława
Mazurkiewicz, Aleksandra
Dudzik, Paulina
Powiązania:
https://bibliotekanauki.pl/articles/1041089.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
dimer
prostatic phosphatase
protein unfolding
Opis:
Kinetics of guanidine hydrochloride (GdnHCl)-induced unfolding of human prostatic acid phosphatase (hPAP), a homodimer of 50 kDa subunit molecular mass was investigated with enzyme activity measurements, capacity for binding an external hydrophobic probe, 1-anilinonaphtalene-8-sulfonate (ANS), accessibility of thiols to reaction with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) and 2-(4'-maleimidylanilino)naphthalene-6-sulfonate (MIANS) and ability to bind Congo red dye. Kinetic analysis was performed to describe a possible mechanism of hPAP unfolding and dissociation that leads to generation of an inactive monomeric intermediate that resembles, in solution of 1.25 M GdnHCl pH 7.5, at 20°C, in equilibrium, a molten globule state. The reaction of hPAP inactivation in 1.25 M GdnHCl followed first order kinetics with the reaction rate constant 0.0715 ± 0.0024 min-1 . The rate constants of similar range were found for the pseudo-first-order reactions of ANS and Congo red binding: 0.0366 ± 0.0018 min-1 and 0.0409 ± 0.0052 min-1, respectively. Free thiol groups, inaccessible in the native protein, were gradually becoming, with the progress of unfolding, exposed for the reactions with DTNB and MIANS, with the pseudo-first-order reaction rate constants 0.327 ± 0.014 min-1 and 0.216 ± 0.010 min-1, respectively. The data indicated that in the course of hPAP denaturation exposure of thiol groups to reagents took place faster than the enzyme inactivation and exposure of the protein hydrophobic surface. This suggested the existence of a catalytically active, partially unfolded, but probably dimeric kinetic intermediate in the process of hPAP unfolding. On the other hand, the protein inactivation was accompanied by exposure of a hydrophobic, ANS-binding surface, and with an increased capacity to bind Congo red. Together with previous studies these results suggest that the stability of the catalytically active conformation of the enzyme depends mainly on the dimeric structure of the native hPAP.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 371-377
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Some biochemical and nutritional studies on the effect of Panax ginseng powder extract on adult Japanese quails
Autorzy:
Osfor, M. M. H.
Powiązania:
https://bibliotekanauki.pl/articles/1373036.pdf
Data publikacji:
1995
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
glucose
serum
alkaline phosphatase
food
liver function
urea
bilirubin
renal function
albumin
lipid
triacylglycerol
physiological parameter
Japanese quail
nutrition
protein
Panax ginseng
blood biochemistry
amino transferase
cholesterol
biochemical parameter
creatinine
Opis:
The effect of the Panax ginseng powder extract on reproduction, growth, renal and liver functions and some blood biochemical indices of Japanese quails were investigated. Panax ginseng powder extract at 2 mg and 4 mg/bird daily increased egg number per hen, average egg weight and hatchability. It slightly improved the efficiency of feed utilization and increased the levels of serum total protein, alkaline phosphatase and aspartate amino transferase (AST). The extract decreased significantly the levels of albumin, total lipids, triacylglycerols, cholesterol and glucose, and had no effect on body weight and the levels of serum bilirubin, urea and creatinine. This suggests that long term studies should be done on many different biochemical and physiological parameters and laboratory animals.
Źródło:
Polish Journal of Food and Nutrition Sciences; 1995, 04, 2; 73-79
1230-0322
2083-6007
Pojawia się w:
Polish Journal of Food and Nutrition Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Interakcje pektynaz w procesie zmian biodostepnosci bialka z paszy dla drobiu
Autorzy:
Mika, M
Wikiera, A
Zyla, K
Perek, P
Powiązania:
https://bibliotekanauki.pl/articles/827262.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Technologów Żywności
Tematy:
pasze przemyslowe
enzymy pektynolityczne
bialko
zywienie zwierzat
przemysl paszowy
preparaty enzymatyczne
fosfatazy
drob
biodostepnosc
pektynaza
enzymy fosfolityczne
industrial feed
pectolytic enzyme
protein
animal feeding
feed industry
enzymatic preparation
phosphatase
poultry
bioavailability
pectinase
phosphorolytic enzyme
Opis:
Badano wpływ enzymów fosforolitycznych i pektynolitycznych na biodostępność białka oraz określono interakcje zachodzące pomiędzy działaniem tych enzymów. Analizy prowadzono z wykorzystaniem metody in vitro, symulującej warunki trawienia w przewodzie pokarmowym ptaków. Wyniki analizowano stosując dwuczynnikową analizę wariancji ANOVA (dwuelementowe kombinacje aktywności enzymatycznych – preparaty: Finase P, Finase AP, Rapidase pomaliq 2F, Energex L). Wykazano, że zarówno dodatek pektynaz, jak i fosfataz do paszy ma istotny wpływ na stężenie białka oznaczanego w dializacie. Ponadto wykazano, że kooperacja z preparatami pektynolitycznymi jest efektywniejsza w przypadku fosfatazy kwaśnej niż fitazy. Stwierdzono także, że wysoka aktywność pektynoesterazy w preparatach pektynolitycznych jest czynnikiem ograniczającym biodostępność białka.
The effects of pectinases and phosphatases on the bioavailability of protein and interactions between these enzymes were studied. Analysis were performed using an in vitro method simulating conditions of the bird’s intestinal digestion tract. The results obtained were analysed using a two way ANOVA variance analysis (two factor combinations of enzymatic activities - the preparations: Finase P, Finase AP, Rapidase pomaliq 2F, and Energex L). The investigations evidenced that the addition of pectinases and phosphatases significantly influenced protein levels being determined in the dializate. Moreover, it was proved that the cooperation with the pectinase preparations was more effective for the acid phosphatase than for the phytase. It was also confirmed that the high pectin esterase activity in pectinase preparations was a factor limiting the protein bioavailability.
Źródło:
Żywność Nauka Technologia Jakość; 2004, 11, 4; 107-116
1425-6959
Pojawia się w:
Żywność Nauka Technologia Jakość
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-13 z 13

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