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1.
001-es BibID:
BIBFORM047051
035-os BibID:
PMID:2157500
Első szerző:
Csortos Csilla (biokémikus)
Cím:
Phosphorylase phosphatase activities of rat liver in streptozotocin-diabetes / Csilla Csortos, Ilona Farkas, Lloyd Sparks, Tamás Bányász, Tibor Kovács, Pál Gergely
Dátum:
1990
ISSN:
0167-4889
Megjegyzések:
Protein phosphatase-1 and 2A, accounting for all the hepatic activity regulating phosphorylase, were assayed in streptozotocin-induced (8 weeks) diabetic Wistar rats. Cytosolic protein phosphatase-1 and 2A were distinguished by chromatography on heparin-Sepharose and by inhibition with inhibitor-2. Approx. 25-35% increases in type-1 phosphorylase phosphatase activity measured in cytosols were registered in diabetic rats when compared with control and 24 h fasting animals. The enrichment of protein phosphatase-1 in the cytosol of streptozotocin-treated rat livers could not be attributed to the reduced glycogen content with the onset of diabetes, since this elevated level of type-1 phosphatase was not observed in fasting rats with low glycogen content. The translocation of type-1 phosphatase from the particulate fraction into the cytosol was also recorded in trypsin-treated samples of diabetic rat livers. The apparent molecular weight of type-1 phosphatase in the cytosol of control and fasted rats was 160,000 as judged by gel filtration. The type-1 phosphatase activity that was released from the particulate fraction by streptozotocin-induced diabetes identified a further enzyme species (Mr 110,000) in the cytosol. Our data imply that the higher levels of cytosolic protein phosphatase-1 in diabetic rat liver could be a consequence of the dissociation of the catalytic subunit of protein phosphatase-1 and the glycogen-binding subunit in rat livers.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Protein phosphatase
Hepatic metabolism
Diabetes
Fasting
Streptozotocin
Rat liver
Megjelenés:
Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1052 : 1 (1990), p. 235-241. -
További szerzők:
Farkas Ilona (1953-) (biokémikus)
Sparks, Lloyd
Bányász Tamás (1960-) (élettanász)
Kovács Tibor (1929-1994) (élettanász)
Gergely Pál (1947-) (biokémikus)
Internet cím:
Intézményi repozitóriumban (DEA) tárolt változat
DOI
Szerző által megadott URL
Borító:
Saját polcon:
2.
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
Borító:
Saját polcon:
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