Subcellular distribution of abnormal proteins in rabbit reticulocytes

Abstract

Inhibitors of ATP synthesis (cyanide, dinitrophenol, fluoride) inhibited proteolysis of pulse-labelled abnormal proteins in rabbit reticulocytes and caused an accumulation of the aberrant polypeptides in the cell debris fraction in a manner analogous to phenylhydrazine-induced Heinz bodies. When the reticulocytes were separated into age-groups by sedimentation through discontinuous gradients of bovine serum albumin, the ability of the cells to degrade puromycin peptides decreased with increasing cellular maturity and, in the more mature cells, up to 40% of the labelled abnormal polypeptide remained associated with the cell debris fraction at the end of the chase period. It is suggested that the association of the abnormal polypeptide with the cell debris fraction is a consequence of a maturation-induced loss, or an inhibitor-induced inactivation of the cellular proteolytic activity.