The predominant form of mammalian DNA topoisomerase I in vivo has a molecular mass of 100 kDa

Scott Samuels, Nobuyoshi Shimizu

Research output: Contribution to journalArticlepeer-review

Abstract

DNA topoisomerase I was purified to apparent homogeneity from human HeLa cells as a single polypeptide with a molecular mass of 100 kDa, as assayed by both gel filtration column chromatography and SDS-polyacrylamide gel electrophoresis. No smaller forms of the enzyme were detected in the purified fraction. Therefore, smaller forms, which have been observed by other investigators, are likely to be the result of proteolysis during isolation and are not relevant to the in vivo activity of DNA topoisomerase I.

Original languageEnglish
Pages (from-to)99-103
Number of pages5
JournalMolecular Biology Reports
Volume19
Issue number2
DOIs
StatePublished - Mar 1994

Keywords

  • HeLa
  • phosphorylation
  • proteolysis
  • purification
  • smaller forms
  • topoisomerase I

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