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  Electron microscopy and image analysis of the multicatalytic proteinase

Baumeister, W., Dahlmann, B., Hegerl, R., Kopp, F., Kühn, L., & Pfeifer, G. (1988). Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Letters., 241(1-2), 239-245.

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Baumeister, W.1, Author              
Dahlmann, B., Author
Hegerl, R.1, Author              
Kopp, F., Author
Kühn, L., Author
Pfeifer, G.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Animal; Cysteine Endopeptidases/ip [Isolation & Purification]; *Cysteine Endopeptidases; Microscopy, Electron; Multienzyme Complexes/ip [Isolation & Purification]; *Multienzyme Complexes; Muscles/en [Enzymology]; Rats; Staining and Labeling; Support, Non-U.S. Gov't
 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.

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 Dates: 1988
 Publication Status: Published in print
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 Identifiers: eDoc: 318369
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Title: FEBS Letters.
Source Genre: Journal
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Pages: - Volume / Issue: 241 (1-2) Sequence Number: - Start / End Page: 239 - 245 Identifier: -