AbstractCanavanine, an arginine analog, is incorporated into HeLa cell protein when cells are incubated in the absence of arginine, and this incorporation can result in the production of nonfunctional enzymes or abnormal proteins. The cells degrade these abnormal proteins up to three times more rapidly than normal cell proteins. The capacity for selective degradation of abnormal proteins is not limited to HeLa cells since human fibroblasts also showed increased degradative rates following exposure to canavanine. In addition, enhanced degradation is not a peculiar property of canavanine incorporation since other amino acid analogs also promoted protein degradation. Thus, mammalian cells have the capacity to recognize and selectively degrade abnormal proteins.
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