Isolation and characterization of hamster brain polyribosome-cytomatrix complexes.
We have developed a method for the isolation of a brain subcellular fraction enriched in both highly aggregated polyribosomes and cytoskeletal proteins. This method is based on gentle dispersion of brain tissue and low speed centrifugation. This fraction is enriched in typical cytoskeletal proteins as glial fibrillary protein, neurofilament proteins and actin. Messenger RNA did not seem to be involved in the polyribosome association to the cytomatrix as shown by the effect of exposure to micrococcal nuclease. On the other hand, in vivo disruption of protein synthesis by acute experimental phenylketonuria, hypothermia or heat-shock did not cause the release of ribosomes from the cytomatrix.
Desjardins
P
P
Département de Chimie et Biochimie, Université de Moncton, N.B., Canada.
Savoie
C
C
Doucet
J
J
Gauthier
D
D
D000199:Actins / Q000302:isolation & purification; D000818:Animals; D001921:Brain / Q000648:ultrastructure*; D002458:Cell Fractionation / Q000379:methods; D002499:Centrifugation, Density Gradient; D006224:Cricetinae; D003598:Cytoskeletal Proteins / Q000302:isolation & purification*; D003599:Cytoskeleton / Q000648:ultrastructure*; D004591:Electrophoresis, Polyacrylamide Gel; D005904:Glial Fibrillary Acidic Protein / Q000302:isolation & purification; D015151:Immunoblotting; D008970:Molecular Weight; D016900:Neurofilament Proteins / Q000302:isolation & purification; D011132:Polyribosomes / Q000648:ultrastructure*
D000199:Actins; D003598:Cytoskeletal Proteins; D005904:Glial Fibrillary Acidic Protein; D016900:Neurofilament Proteins