CCL

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001-es BibID:BIBFORM029040
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Purification and characterization of three distinct types of protein phosphatase catalytic subunits in bovine platelets / Ferenc Erdődi, Csilla Csortos, Lloyd Sparks, Andrea Murányi, Pál Gergely
Dátum:1992
ISSN:0003-9861
Megjegyzések:The catalytic subunits of bovine platelet protein phosphatases were separated into three distinct forms by chromatography on heparin-Sepharose. Each phosphatase was further purified to apparent homogeneity as judged in sodium dodecyl sulfate-polyacrylamide gel yielding single protein bands of 37, 41, and 36 kDa. The 37-kDa phosphatase was excluded from heparin-Sepharose and preferentially dephosphorylated the alpha-subunit of phosphorylase kinase. It was stimulated by polycations (polybrene or histone H1) and was inhibited by okadaic acid (IC50 = 0.3 nM), but its activity was not influenced by inhibitor-2 or heparin. The 41-kDa phosphatase was eluted from heparin-Sepharose by 0.20-0.25 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was stimulated by polycations and inhibited by okadaic acid (IC50 = 2 nM), but its activity was not affected by inhibitor-2 or heparin. The 36-kDa phosphatase was eluted from heparin-Sepharose by 0.45-0.50 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was inhibited by inhibitor-2, heparin, histone H1, and okadaic acid (IC50 = 70 nM). The 37- and 36-kDa phosphatases can be classified as type-2A and type-1 enzymes, respectively. The 41-kDa phosphatase does not precisely fit the criteria of either type, showing only partial similarities to both type-1 and type-2A enzymes and it may represent a novel type of protein phosphatase in bovine platelets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Archives of Biochemistry And Biophysics. - 298 : 2 (1992), p. 682-687. -
További szerzők:Sparks, Lloyd Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus) Murányi Andrea (1966-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM003560
Első szerző:Kókai Endre (biokémikus, biológus)
Cím:CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y / Kókai E., Tantos Á., Vissi E., Szöőr B., Tompa P., Gausz J., Alphey L., Friedrich P., Dombrádi V.
Dátum:2006
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatases Y
protein-protein interaction
CG15031 gene product
heat-stable unstructured RNA-binding protein
Drosophila melanogaster
intrinsically unstructured protein
protein phosphorylation
Megjelenés:Archives of Biochemistry and Biophysics. - 451 : 1 (2006), p. 59-67. -
További szerzők:Tantos Ágnes Vissi Emese (1968-) (biokémikus, biológus) Szöőr Balázs (1966-) (biokémikus) Tompa Péter Gausz János Alphey, Luke Friedrich Péter Dombrádi Viktor (1953-) (biokémikus)
Internet cím:elektronikus változat
DOI
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3.

001-es BibID:BIBFORM027917
Első szerző:Vissi Emese (biokémikus, biológus)
Cím:Protein phosphatase 1 catalytic subunit isoforms from alfalfa : biochemical characterization and cDNA cloning / Emese Vissi, Éva Csordás Tóth, Izabella Kovács, Zoltán Magyar, Gábor V. Horváth, Péter Bagossi, Pál Gergely, Dénes Dudits, Viktor Dombrádi
Dátum:1998
Megjegyzések:The catalytic subunit of protein phosphatase 1 (PP1c) was purified from an alfalfa (Medicago sativa) microcallus cell culture. The preparation was inhibited by rabbit muscle inhibitor-2 and okadaic acid and had a molecular mass of 35 kDa. Five distinct cDNAs termed MsPP1alpha, -beta, -gamma, -delta, and -epsilon were cloned from a M. sativa somatic embryo library. MsPP1alpha was identical to a cDNA reported earlier [A. Páy, M. Pirck, L. Bögre, H. Hirt, and E. Heberle-Bors Mol. Gen. Genet. 244, 176-182, 1994], while the others represented novel isoforms encoded by separate genes. The predicted amino acid sequences of MsPP1alpha, -beta, -gamma, -delta, and -epsilon were highly similar to each other and to other known PP1c sequences. The GST-MsPP1ss fusion protein expressed in Escherichia coli was catalytically active and was inhibited by inhibitor-2 and okadaic acid. Affinity-purified polyclonal MsPP1antipeptide antibody detected a protein of 36 kDa in crude cell extracts. These results proved that the cDNA clone encoded an active PP1c which was very similar to the purified enzyme. The mRNA and protein concentrations of PP1c as well as the specific activity of protein phosphatase 1 did not change during the cell cycle in a synchronized alfalfa cell culture. On the other hand, the isoforms exhibited different steady-state mRNA levels in different plant organs suggesting tissue-specific functions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatase1
Medicago sativa
protein purification
cDNA sequencing
cell cycle
gene expression
egyetemen (Magyarországon) készült közlemény
Megjelenés:Archives of Biochemistry and Biophysics. - 360 : 2 (1998), p. 206-214. -
További szerzők:Csordás Tóth Éva Kovács Izabella (Szeged) Magyar Zoltán Horváth Gábor V. Bagossi Péter (1966-2011) (biokémikus, vegyész) Dudits Dénes Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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