Degradation of thialysine- or selenalysine-containing abnormal proteins in CHO cells.
CHO cells can incorporate thialysine and selenalysine in their proteins in substitution of lysine. Data are reported in the present paper showing that proteins containing either thialysine or selenalysine are unstable and quite rapidly degraded. The degradation rate is strictly related to the extent of protein lysine substitution. At similar extent of substitution, selenalysine-containing proteins are more unstable that thialysine-containing ones.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002478:Cells, Cultured; D006224:Cricetinae; D003412:Cricetulus; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D007532:Isoleucine / Q000378:metabolism; D007930:Leucine / Q000378:metabolism; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D016566:Organoselenium Compounds; D014176:Protein Biosynthesis; D011492:Protein Hydrolysates / Q000032:analysis; D011506:Proteins / Q000378:metabolism*; D012643:Selenium / Q000378:metabolism*
D000596:Amino Acids; D016566:Organoselenium Compounds; D011492:Protein Hydrolysates; D011506:Proteins; D007532:Isoleucine; C000204:S-2-aminoethyl cysteine; C011351:selenalysine; D007930:Leucine; D012643:Selenium; D008239:Lysine; D003545:Cysteine