Electron microscopy and image analysis of the multicatalytic proteinase

FEBS Lett. 1988 Dec 5;241(1-2):239-45. doi: 10.1016/0014-5793(88)81069-x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cysteine Endopeptidases* / isolation & purification
  • Microscopy, Electron
  • Multienzyme Complexes* / isolation & purification
  • Muscles / enzymology
  • Proteasome Endopeptidase Complex
  • Rats
  • Staining and Labeling

Substances

  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex