Breakdown of aberrant protein in rabbit reticulocytes decreases with cell age.
Rabbit reticulocytes, separated into ten cell age groups by bovine serum albumin density-gradient sedimentation, were pulse-labelled with [14C]leucine in the presence of either puromycin dihydrochloride or aminoethyl-L-cysteine (a lysine analogue). Intracellular proteolysis of both the puromyucinyl-peptides and analogue-containing protein decreased with cell maturity.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D003545:Cysteine / Q000031:analogs & derivatives / Q000378:metabolism; D011691:Puromycin / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism* / Q000502:physiology; D012710:Serum Albumin, Bovine
D001798:Blood Proteins; D012710:Serum Albumin, Bovine; C000204:S-2-aminoethyl cysteine; D011691:Puromycin; D003545:Cysteine