[Effect of postmortem autolysis on the 40S ribosomal subunit proteins of rat skeletal muscles].
A ribosomal protein component was impaired during autolysis of 40S subunits, obtained from polysomes of autolysed muscles using KCL-puromycine method. These 40S subunits exhibited higher buoyant density as compared with controls. For the direct analysis the ribosomal proteins were extracted from 40S subunits by 66% acetic acid containing 0.01 M MgCl2 and fractionated using one- and two-dimensional polyacrylamide gel electrophoresis. The data obtained suggest that some proteins were hydrolyzed by proteolytic enzymes during autolysis: assumption of dissociation into the subunits of 6 of the ribosomal proteins during autolysis does not account for the phenomena observed.
D000818:Animals; D001329:Autolysis / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D009132:Muscles / Q000378:metabolism*; D051381:Rats; D012269:Ribosomal Proteins / Q000378:metabolism*
D012269:Ribosomal Proteins
Vliianie posmertnogo avtoliza na belki 40S ribosomnykh sub"edinits skeletnykh myshts krys.