Electron microscopy of native and reconstituted alpha crystallin aggregates.
The size and shape of native alpha crystallin aggregates extracted at either 4 degrees C (alpha c-crystallin) or 37 degrees C (alpha m-crystallin), were compared with each other, as well as with aggregates reconstituted from either pure alpha A or alpha B subunits using electron microscopy. The alpha B aggregates were the most uniform in size (about 9 nm in diameter) and the best stained. alpha A particles were about the same size as the alpha B, but the population distribution was broader and some indication of interparticle association was observed. alpha c particles exhibited a bimodal distribution, with one peak greater than the reconstituted particles and the other about the same size; alpha m was smaller than the reconstituted structures.
Koretz
J F
JF
Center for Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Augusteyn
R C
RC
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000032:analysis*; D008854:Microscopy, Electron; D008968:Molecular Conformation
D003459:Crystallins