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001-es BibID:	BIBFORM028159
Első szerző:	Bakó Éva (biokémikus)
Cím:	Purification and partial characterization of protein phosphatases from rat thymus / Éva Bakó, Viktor Dombrádi, Ferenc Erdődi, Lawrence Zumo, Pál Kertai, Pál Gergely
Dátum:	1989
ISSN:	0167-4889
Megjegyzések:	Protein phosphatases assayed with phosphorylase alpha are present in the soluble and particulate fractions of rat thymocytes. Phosphorylase phosphatase activity in the cytosol fraction was resolved by heparin-Sepharose chromatography into type-1 and type-2A enzymes. Similarities between thymocyte and muscle or liver protein phosphatase-1 included preferential dephosphorylation of the beta subunit of phosphorylase kinase, inhibition by inhibitor-2 and retention by heparin-Sepharose. Similarities between thymocyte and muscle or liver protein phosphatase-2A included specificity for the alpha subunit of phosphorylase kinase, insensitivity to the action of inhibitor-2, lack of retention by heparin-Sepharose and stimulation by polycationic macromolecules such as polybrene, protamine and histone H1. Protein phosphatase-1 from the cytosol fraction of thymocytes had an apparent molecular mass of 120 kDa as determined by gel filtration. The phosphatase-2A separated from the cytosol of thymocytes may correspond to phosphatase-2A0, since it was completely inactive (latent) in the absence of polycation and had activity only in the presence of polycations. The apparent molecular mass of phosphatase-2A0 from thymocytes was 240 kDa as determined by gel filtration. The catalytic subunit of thymocyte type-1 protein phosphatase was purified with heparin-Sepharose chromatography followed by gel filtration and fast protein liquid chromatography on Mono Q column. The purified type-1 catalytic subunit exhibited a specific activity of 8.2 U/mg and consisted of a single protein of 35 kDa as judged by SDS-gel electrophoresis. The catalytic subunit of type-2A phosphatase from thymocytes appearing in the heparin-Sepharose flow-through fraction was further purified on protamine-Sepharose, followed by gel filtration. The specific activity of the type-2A catalytic subunit was 2.1 U/mg and consisted of a major protein of 34.5 kDa, as revealed by SDS-gel electrophoresis.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban protein phosphatase-1 protein phosphatase-2A polycation heparin-Sepharose thymocyte rat egyetemen (Magyarországon) készült közlemény
Megjelenés:	Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1013 : 3 (1989), p. 300-305. -
További szerzők:	Kertai Pál (1927-2016) (népegészségügyi szakember) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Zumo, Lawrence (1966-) Gergely Pál (1947-) (biokémikus)
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001-es BibID:	BIBFORM029042
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Dephosphorylation of distinct sites in myosin light chain by two types of phosphatase in aortic smooth muscle / Ferenc Erdődi, Anikó Rokolya, Michael Bárány, Kate Bárány
Dátum:	1989
ISSN:	0167-4889
Megjegyzések:	Two types of myosin light chain phosphatase from aortic smooth muscle extract were separated by chromatography on heparin-agarose. The phosphatase which appeared in the flow-through fractions had low activity on actomyosin, its apparent molecular mass was 260 kDa and upon ethanol treatment it generated a catalytic subunit with an apparent molecular mass of 36-39 kDa as determined by gel filtration. This phosphatase preferentially dephosphorylated the alpha-subunit of phosphorylase kinase and its phosphorylase phosphatase activity was not inhibited by heparin, inhibitor-1 or inhibitor-2. The phosphatase retained by heparin-agarose had high activity on actomyosin, its apparent molecular mass was 150 kDa and upon ethanol treatment it generated a catalytic subunit with an apparent molecular mass of 39-42 kDa. It preferentially dephosphorylated the beta-subunit of phosphorylase kinase and its phosphorylase phosphatase activity was not inhibited by heparin, inhibitor-1 or inhibitor-2. Myosin light chain was phosphorylated by myosin light chain kinase in peptides AB (Ser-P) and CD (Thr-P), and/or by protein kinase C in peptides E (Ser-P) and F (Thr-P) as determined by one-dimensional phosphopeptide mapping. The catalytic subunit of heparin-agarose flow-through phosphatase preferentially dephosphorylated peptide F over peptides AB, CD and E in both isolated light chain and actomyosin. The catalytic subunit of heparin-agarose bound phosphatase could effectively dephosphorylate all sites in isolated light chain, whereas it was less effective on dephosphorylation of peptide E in actomyosin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény Myosin light chain Multiple phosphorylation Myosin light chain phosphatase Aortic smooth muscle
Megjelenés:	Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1011 : 1 (1989), p. 67-74. -
További szerzők:	Rokolya Anikó Bárány Mihály Bárány Katalin
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001-es BibID:	BIBFORM075940
Első szerző:	Kiss Andrea (biokémikus, vegyész)
Cím:	Myosin phosphatase : unexpected functions of a long-known enzyme / Kiss Andrea, Erdődi Ferenc, Lontay Beáta
Dátum:	2019
ISSN:	0167-4889
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1866 : 1 (2019), p. 2-15. -
További szerzők:	Erdődi Ferenc (1953-) (biokémikus) Lontay Beáta (1975-) (biokémikus)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00044 GINOP EFOP-3.6.2-16-2017-00006 EFOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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