ausblenden:
Schlagwörter:
Animal; *Archaea/en [Enzymology]; *Bacteria/en [Enzymology]; Calcium Chloride/pd [Pharmacology]; Chromatography; Comparative Study; *Cysteine Endopeptidases/ip [Isolation & Purification]; Cysteine Endopeptidases/me [Metabolism]; Electrophoresis, Polyacrylamide Gel; Evolution; Macromolecular Systems; Microscopy, Electron; Molecular Weight; *Multienzyme Complexes/ip [Isolation & Purification]; Multienzyme Complexes/me [Metabolism]; Muscles/en [Enzymology]; Peptide Fragments; Rats; Substrate Specificity; Support, Non-U.S. Gov't
Zusammenfassung:
From the thermoacidophilic archaebacterium, Thermoplasma acidophilum, a proteolytically active particle has been isolated which is almost identical in size and shape with the multicatalytic proteinase (prosome) from rat. This result indicates that prosomes have been developed early in evolution and that they possibly serve functions common to all living cells.
