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001-es BibID:	BIBFORM028262
Első szerző:	Dombrádi Viktor (biokémikus)
Cím:	The association of phosphorylase kinase with rabbit muscle T-tubules / V. Dombrádi, S. R. Silberman, E. Y. C. Lee, A. H. Caswell, N. R. Brandt
Dátum:	1984
ISSN:	0003-9861
Megjegyzések:	Evidence is presented for the association of a phosphorylase kinase activity with transverse tubules as well as terminal cisternae in triads isolated from rabbit skeletal muscle. This activity remained associated with T-tubules throughout the purification of triad junctions by one cycle of dissociation and reassociation. The possibility that the presence of phosphorylase kinase in these highly purified membrane vesicle preparations was due to its association with glycogen was eliminated by digestion of the latter with alpha-amylase. The phosphorylase kinase activity associated with the T-tubule membranes was similar to that reported for other membrane-bound phosphorylase kinases. The enzyme had a high pH 6.8/pH 8.2 activity ratio (0.4-0.7) and a high level of Ca2+ independent activity (EGTA/Ca2+ = 0.3-0.5). The kinase activated and phosphorylated exogenous phosphorylase b with identical time courses. When mechanically disrupted triads were centrifuged on continuous sucrose gradients, the distribution of phosphorylase kinase activity was correlated with the distribution of a Mr 128,000 polypeptide in the gradients. This polypeptide and a Mr 143,000 polypeptide were labeled with 32P by endogenous and exogenous protein kinases. These findings suggest that the membrane-associated phosphorylase kinase may be similar to the cytosolic enzyme. Markers employed for the isolated organelles included a Mr 102,000 membrane polypeptide which followed the distribution of Ca2+-stimulated 3-O-methylfluorescein phosphatase activity, which is specific for the sarcoplasmic reticulum. A Mr 72,000 polypeptide was confirmed to be a T-tubule-specific protein. Several proteins of the triad component organelle were phosphorylated by the endogenous kinase in a Ca2+/calmodulin-stimulated manner, including a Mr ca. 72,000 polypeptide found only in the transverse tubule.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban phosphorylase kinase T-tubule külföldön készült közlemény
Megjelenés:	Archives Of Biochemistry And Biophysics. - 230 : 2 (1984), p. 615-630. -
További szerzők:	Silberman, Steven R. Lee, Ernest Y. C. Caswell, A. H. Brandt, N. R.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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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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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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