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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
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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