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001-es BibID:	BIBFORM028259
Első szerző:	Dombrádi Viktor (biokémikus)
Cím:	Purification and characterization of glycogen phosphorylase from Drosophila melanogaster / V. Dombrádi, J. Hajdú, P. Friedrich, G. Bot
Dátum:	1985
Megjegyzések:	Glycogen phosphorylase View the MathML source was purified from Drosophila melanogaster with a yield of 15% by low speed centrifugation, DEAE-Sepharose CL-6B chromatography and affinity chromatography on 5-AMP-Sepharose 4B. The preparation proved to be homogeneous by SDS-polyacrylamide gel electrophoresis and showed a subunit molecular weight of 95,000. Gel filtration of the native enzyme on Sephacryl S-300 revealed a molecular weight of 176,000 suggesting that phosphorylase View the MathML source is a dimer composed of two identical subunits. The fruit fly phosphorylase View the MathML source has a maximal specific activity of 36 U/mg when assayed in the direction of glycogen synthesis. It requires AMP for activity (View the MathML source mM, Hill coefficient: 1.8). The View the MathML source for glycogen is 0.4% and the View the MathML source for glucose-1-phosphate is 20 mM (Hill coefficient: 1.3). The enzyme is inhibited by glucose, UDPG, caffeine, glucose-6-phosphate, ATP and IMP.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Drosophila melanogaster glycogen phosphorylase b isolation molecular weight kinetic properties egyetemen (Magyarországon) készült közlemény
Megjelenés:	Insect Biochemistry. - 15 : 3 (1985), p. 403-410. -
További szerzők:	Hajdu János Friedrich Péter Bot György (1917-1998) (biokémikus, vegyész)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM028256
Első szerző:	Dombrádi Viktor (biokémikus)
Cím:	Regulation of glycogen phosphorylase in Drosophila melanogaster by reversible phosphorylation-dephosphorylation / V. Dombrádi, P. Dévay, P. Friedrich, G. Bot
Dátum:	1986
Megjegyzések:	Homogeneous glycogen phosphorylase b purified from Drosophila melanogaster was activated by phosphorylase kinase isolated from rabbit skeletal muscle. The activation generated phosphorylase a containing 1.1 ± 0.1 phosphoryl group per subunit. Phosphorylase a prepared in this way had a s20w = 8.5S and a subunit molecular mass of 95,000. It could be inactivated (dephosphorylated) by the catalytic subunit of rabbit muscle protein phosphatase-1. The activation-inactivation of phosphorylase by endogenous phosphorylase kinase and phosphatase was also demonstrated in crude homogenates of D. melanogaster. The main protein phosphorylated in the fruit fly homogenate comigrated with purified Drosophila phosphorylse a in sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Phosphate incorporation into this protein was correlated with phosphorylase activation. Phosphorylase was partially purified from flies fed on [32P]phosphate by 5-AMP Sepharose affinity chromatography. SDS gel electrophoresis followed by autoradiography revealed that it was phosphorylated in vivo. 20 ± 5% of the total phosphorylase was found to be in the active a form in the anaesthetized insects. Our findings indicate that Drosophila phosphorylase undergoes reversible phosphorylation-dephosphorylation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Drosophila melanogaster protein phosphorylation regulatioin glycogen phosphorylase a glycogen phosphorylase b egyetemen (Magyarországon) készült közlemény
Megjelenés:	Insect Biochemistry. - 16 : 3 (1986), p. 557-565. -
További szerzők:	Dévay Piroska Friedrich Péter Bot György (1917-1998) (biokémikus, vegyész)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM028164
Első szerző:	Dombrádi Viktor (biokémikus)
Cím:	Regulation of phosphorylase kinase in Drosophila melanogaster / V. Dombrádi, V. Risnik, F. Erdődi, G. Bot, P. Friedrich
Dátum:	1987
Megjegyzések:	The regulation of phosphorylase kinase has been studied in crude homogenates of adult flies and larval brains of Drosophila melanogaster. The kinase has an alkaline pH optimum (about pH 8.6), is inhibited by an excess of Mg2+ and is stimulated by Ca2+ in the homogenates. Incubation of larval brains with octopamine, especially in the presence of theophylline, or with forskolin, markedly elevated the level of cAMP with no, or marginal, activation of phosphorylase. In contrast, Ca2+ in the presence of A-23187 caused a two-fold increase in phosphorylase View the MathML source. The mutant dunceM11 flies contain six to seven times as much cAMP as the wild type Canton-S flies and have a somewhat elevated phosphorylase View the MathML source level.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban phosphorylase kinase glycogen phosphorylase calcium ion cyclic AMP Drosophila egyetemen (Magyarországon) készült közlemény
Megjelenés:	Insect Biochemistry. - 17 : 4 (1987), p. 579-585. -
További szerzők:	Risnik V. Friedrich Péter Erdődi Ferenc (1953-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM051766
035-os BibID:	PMID:24727027
Első szerző:	Kerekes Éva (Ph.D hallgató)
Cím:	Functional analysis of the glycogen binding subunit CG9238/Gbs-70E of protein phosphatase 1 in Drosophila melanogaster / Éva Kerekes, Endre Kókai, Ferenc Sándor Páldy, Viktor Dombrádi
Dátum:	2014
ISSN:	0965-1748
Megjegyzések:	The product of the CG9238 gene that we termed glycogen binding subunit 70E (Gbs-70E) was characterized by biochemical and molecular genetics methods. The interaction between Gbs-70E and all catalytic subunits of protein phosphatase 1 (Pp1-87B, Pp1-9C, Pp1-96A and Pp1-13C) of Drosophila melanogaster was confirmed by pairwise yeast two-hybrid tests, co-immunoprecipitation and pull down experiments. The binding of Gbs-70E to glycogen was demonstrated by sedimentation analysis. With RT-PCR we found that the mRNAs coding for the longer Gbs-70E PB/PC protein were expressed in all developmental stages of the fruit flies while the mRNA for the shorter Gbs-70E PA was restricted to the eggs and the ovaries of the adult females. The development specific expression of the shorter splice variant was not conserved in different Drosophila species. The expression level of the gene was manipulated by P-element insertions and gene deletion to analyze the functions of the gene product. A small or moderate reduction in the gene expression resulted in no significant changes, however, a deletion mutant expressing very low level of the transcript lived shorter and exhibited reduced glycogen content in the imagos. In addition, the gene deletion decreased the fertility of the fruit flies. Our results prove that Gbs-70E functions as the glycogen binding subunit of protein phosphatase 1 that regulates glycogen content and plays a role in the development of eggs in D. melanogaster.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban CG9238 Drosophila melanogaster Fertility Gbs-70E Glycogen binding targeting subunit Glycogen content Longevity Protein phosphatase 1 Doktori iskola
Megjelenés:	Insect Biochemistry and Molecular Biology. - 49 (2014), p. 70-79. -
További szerzők:	Kókai Endre (1971-) (biokémikus, biológus) Páldy Ferenc Sándor Dombrádi Viktor (1953-) (biokémikus)
Pályázati támogatás:	TÁMOP-4.2.2/B-10/1-2010-0024 TÁMOP Molekuláris Orvostudomány Doktori Iskola
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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