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001-es BibID:	BIBFORM029382
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Autophosphorylation of phosphorylase kinase and its regulatory function in the dephosphorylation of phosphorylase A / F. Erdődi, Éva Bakó, G. Bot, P. Gergely
Dátum:	1987
Megjegyzések:	Autophosphorylation of phosphorylase kinase was measured under conditions that favoured autoactivation. Heparin and troponin C stimulated the autophosphorylation of phosphorylase kinase at pH 6.8 in a Ca2+-dependent manner. The concentration required for the half-maximal stimulation of autophosphorylation for calcium ions was 2 microM in the absence of effectors, whereas 0.7 microM and 0.1 microM in the presence of troponin C and heparin, respectively. Calmodulin increased the rate of autophosphorylation of the alpha subunit only, resulting in a slight increase in the rate of autoactivation of phosphorylase kinase. Troponin C, heparin and polybrene enhanced the rate of autophosphorylation of both alpha and beta subunits. The increased autophosphorylation coincided with an enhancement of kinase activity. Neither of these stimulatory macromolecules had significant influence on the total number of phosphate groups incorporated into the alpha or beta subunits by autophosphorylation. Thio-autophosphorylated form of phosphorylase kinase behaved as an inhibitor in the dephosphorylation of phosphorylase a by the catalytic subunits of phosphatase-1 or phosphatase-2A and by the latent form of phosphatase-2A. Concentration of phosphorylase kinase needed to 50% inhibition was in the range of 0.05-0.08 microM.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény hazai lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Acta Biochimica et Biophysica Hungarica. - 22 : 4 (1987), p. 425-438. -
További szerzők:	Bakó Éva (1958-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM047052
035-os BibID:	PMID:2854691
Első szerző:	Farkas Ilona (biokémikus)
Cím:	Activation/dephosphorylation of rabbit muscle glycogen synthase by the catalytic subunits of protein phosphatase-1 and 2A / Ilona Farkas, B. Tóth, Gy. Vereb, Csilla Csortos, P. Gergely
Dátum:	1988
ISSN:	0237-6261
Megjegyzések:	Glycogen synthase a was purified from rabbit skeletal muscle by a procedure involving heparin-Sepharose chromatography. Glycogen synthase a was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase to give synthase b1. Dephosphorylation and activation of synthase b1 was investigated using the catalytic subunits of protein phosphatase-1 and 2A. The dephosphorylation and activation of synthase b1 was biphasic with a larger rate constant for the initial phase. Analysis of tryptic phosphopeptides of glycogen synthase during the course of dephosphorylation revealed a faster initial phosphate release from site-2 by both phosphatases comparing to sites-1a and 1b. Ligand effects on synthase phosphatase reactions were also studied. Spermine was found to inhibit protein phosphatase-1 activity and to stimulate type-2A phosphatase using synthase b1 as substrate.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Acta Biochimica et Biophysica Hungarica. - 23 : 3-4 (1988), p. 231-246. -
További szerzők:	Tóth Béla (1954-) (vegyész, biokémikus) Vereb György (1938-) (biokémikus, sejtbiológus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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