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001-es BibID:	BIBFORM029044
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Phosphorylation of the 20,000-Da myosin light chain isoforms of arterial smooth muscle by myosin light chain kinase and protein kinase C / Ferenc Erdődi, Anikó Rokolya, Michael Bárány, Kate Bárány
Dátum:	1988
ISSN:	0003-9861
Megjegyzések:	Phosphorylation of myosin light chain (LC) isoforms in arterial actomyosin can be induced by endogenous kinases upon addition of Mg2+ and ATP. The extent of phosphorylation in the presence of 2 mM ethylene glycol bis(beta-aminoethyl ether)N,N'-tetraacetic acid (EGTA), 0.2 mM Ca2+, or 0.2 mM Ca2+ plus calmodulin is 1.6, 2.1, and 2.3 mol phosphate/mol LC, respectively. Two-dimensional gel electrophoresis of actomyosin shows that the LC isoforms may be mono-, di-, and triphosphorylated. Tryptic phosphopeptide mapping of LC indicates that the radioactive phosphate is distributed to six peptides referred to as A through F. Phosphoamino acid analyses and the phosphopeptide maps of isolated LC, phosphorylated by either purified myosin light chain kinase or protein kinase C, reveal that myosin light chain kinase phosphorylates a serine residue in peptides A and B, and threonine plus serine residues in peptides C and D. Peptides E and F are phosphorylated by protein kinase C in serine and threonine residues, respectively. In actomyosin, with EGTA, phosphorylation of peptides E and F proceeds while phosphorylation of peptides A, B, C, and D is inhibited. Ca2+ and calmodulin enhance the phosphorylation of peptides A, B, C, and D, while phosphorylation of peptides E and F is decreased. In isolated LC, myosin light chain kinase preferentially phosphorylates the peptides A and B over C and D. Phosphorylation of peptides E and F in LC by protein kinase C promotes additional phosphorylation of peptides C and D by myosin light chain kinase, whereas phosphorylation of peptides A and B is diminished. The present data suggest that the phosphorylation of distinct sites in arterial myosin light chain by myosin light chain kinase and protein kinase C is interrelated.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Archives of Biochemistry And Biophysics. - 266 : 2 (1988), p. 583-591. -
További szerzők:	Rokolya Anikó Bárány Mihály Bárány Katalin
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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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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