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PMID: 2461878 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Electron microscopy and image analysis of the multicatalytic proteinase.

FEBS letters ·Vol. 241 ·No. 1-2 ·1988-12-05 ·Pages 239-45

Baumeister W, Dahlmann B, Hegerl R, Kopp F, Kuehn L, Pfeifer G

Abstract

One electron micrographs, negatively stained multicatalytic proteinase molecules are viewed end-on (ring shaped) or side-on (rectangular shaped). For aurothioglucose, ammonium molybdate- and phosphotungstate-stained molecules, the dimensions measured are consistent. In contrast, uranyl acetate-staining reveals ring-shaped particles which vary in diameter between 12 and 16 nm. This is due to a partial collapse and substantial flattening of the structure. Digital image analysis of side-on views of the particles reveals a tripartite, reel-shaped structure. Within the ring-like, end-on projections of ammonium molybdate-stained molecules six local centres of mass can be discerned; their position appears to depart, however, from a true six-fold symmetry.

MeSH Terms
Animals Cysteine Endopeptidases/isolation & purification Microscopy, Electron Multienzyme Complexes/isolation & purification Muscles/enzymology Proteasome Endopeptidase Complex Rats Staining and Labeling
Chemicals
Multienzyme Complexes Cysteine Endopeptidases Proteasome Endopeptidase Complex
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Baumeister W
Max-Planck-Institut für Biochemie, Martinsried, FRG.
Dahlmann B
Hegerl R
Kopp F
Kuehn L
Pfeifer G
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1988-12-05
Pages
239-45
Language
English
Region
England
NLM ID
0155157
Subset
IM
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