Degradation of abnormal proteins in HeLa cells.
The experiments show that abnoramal proteins are degraded faster than normal ones in HeLa cells. Among the fragmentary proteins made in the presence of puromycin, those with low molecular weight are least stable. Proteins made after incubation with 5-fluorouracil or in the presence of some amino acid analogues are also unstable. Breakdown of proteins made in the presence or absence of puromycin is nearly unaffected by cycloheximide and is independent of pH between 7 and 8.
D000596:Amino Acids / Q000494:pharmacology; D000814:Aniline Compounds / Q000494:pharmacology; D002172:Canavanine / Q000494:pharmacology; D005001:Ethionine / Q000494:pharmacology; D005472:Fluorouracil / Q000494:pharmacology; D006367:HeLa Cells; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000378:metabolism*; D011422:Propionates / Q000494:pharmacology; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism; D011691:Puromycin / Q000494:pharmacology*; D014364:Tryptophan / Q000031:analogs & derivatives / Q000494:pharmacology; D010135:p-Fluorophenylalanine / Q000494:pharmacology
D000596:Amino Acids; D000814:Aniline Compounds; D009363:Neoplasm Proteins; D011422:Propionates; D011506:Proteins; D002172:Canavanine; D011691:Puromycin; D010135:p-Fluorophenylalanine; D014364:Tryptophan; D005472:Fluorouracil; D005001:Ethionine