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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Changes in proteinase and peptidase activities during reticulocyte maturation.

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.[1]

References

  1. Changes in proteinase and peptidase activities during reticulocyte maturation. McKay, M.J., Atkinson, E.M., Worthington, V.C., Hipkiss, A.R. Biochim. Biophys. Acta (1983) [Pubmed]
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