Premium
Subcellular distribution of abnormal proteins in rabbit reticulocytes
Author(s) -
Daniels R.S.,
McKay M.J.,
Atkinson E.M.,
Hipkiss A.R.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80266-x
Subject(s) - proteolysis , puromycin , biochemistry , bovine serum albumin , phenylhydrazine , chemistry , spectrin , cell fractionation , cell , albumin , trichloroacetic acid , biology , protein biosynthesis , cytoskeleton , enzyme , medicinal chemistry
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.