de.mpg.escidoc.pubman.appbase.FacesBean
Deutsch
 
Hilfe Wegweiser Impressum Kontakt Einloggen
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Evidence for the existence of both proteasomes and a novel high molecular weight peptidase in entamoeba histolytica

MPG-Autoren
Es sind keine MPG-Autoren in der Publikation vorhanden
Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Scholze, H., Frey, S., Cejka, Z., & Bakkergrunwald, T. (1996). Evidence for the existence of both proteasomes and a novel high molecular weight peptidase in entamoeba histolytica. Journal of Biological Chemistry, 271(11), 6212-6216.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-72F3-9
Zusammenfassung
To screen for high molecular weight proteases in Entamoeba histolytica, we subjected a soluble amebal extract to density gradient centrifugation and tested the fractions for activity against the chymotryptic peptide substrate, Suc-leucyl-leucyl-valyl-tyrosyl-4-methylcoumaryl-7-amide. Two peaks of activity, of approximately 11 and 20 S, were clearly separated. Based on SDS-electrophoretic pattern and immunoblot analysis, we ascribe the 20 S activity to proteasomes. The 11 S protein was purified from amebal homogenates by a series of chromatographic steps. As determined by molecular sieve chromatography and nondenaturing gel electrophoresis, the native complex had an apparent M(r) of 385,000 +/- 10%. On SDS gels, the purified enzyme exhib ited a single band of M(r) 62,000 that yielded a single N-terminal sequence, indicating that the preparation was homogeneous and that the native complex consisted of six very similar or identical subunits. The enzyme preferred peptides with aromatic residues at the P-1 position and had low but distinct activity toward azocasein. We conclude that the 11 S enzyme is a novel high molecular weight protease that is distinct from proteasomes. [References: 31]