McKay M J, Atkinson E M, Worthington V C, Hipkiss A R
Biochim Biophys Acta. 1983 Aug 23;759(1-2):42-8. doi: 10.1016/0304-4165(83)90187-3.
The ability of rabbit reticulocytes to degrade puromycin-peptides and aminoethylcysteine-induced aberrant polypeptides decreased during cellular maturation. Cell-free studies indicate that the fall in proteolytic activity is not a consequence of accumulation of proteinase inhibitors or the conversion of all of the abnormal protein into undegradable forms. A decrease in peptidase activity using seven dipeptides and one tripeptide as substrates was also found to accompany reticulocyte maturation. Addition of the aminopeptidase B inhibitor bestatin to reticulocyte extracts did not inhibit the conversion of acid-precipitable puromycin-peptides to acid-soluble products; bestatin did induce the accumulation of very low molecular weight material (possibly di- or tripeptides) within the acid soluble fraction.
