Restriction endonuclease AfaI from Acidiphilium facilis, a new isoschizomer of RsaI: purification and properties

Dexian Dou, Kenji Inagaki, Keiko Kita, Atsushi Ohshima, Nobutugu Hiraoka, Noriaki Kishimoto, Tsuyoshi Sugio, Tatsuo Tano

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

We have purified AfaI endonuclease, an isoschizomer of RsaI, from Acidiphilium facilis strain 28H. The enzyme is homogeneous as judged by polyacrylamide gel electrophoresis, and composed of a single polypeptide chain with a molecular weight of 30 000. AfaI endonuclease, like RsaI, recognizes the tetranucleotide sequence 5′-G-T-A-C-3′, and cleaves between the T and A to produce blunt-ended fragments. The yield of the enzyme is 50-100-times that of the RsaI, which is form a phototrophic bacterium, Rhodospseudomonas sphaeroides strain 28/5.

Original languageEnglish
Pages (from-to)83-86
Number of pages4
JournalBBA - Gene Structure and Expression
Volume1009
Issue number1
DOIs
Publication statusPublished - Sep 21 1989

Keywords

  • (A. facilis)
  • Acidophilic bacterium
  • Enzyme purification
  • Isoschizomer
  • Restriction endonuclease

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Fingerprint Dive into the research topics of 'Restriction endonuclease AfaI from Acidiphilium facilis, a new isoschizomer of RsaI: purification and properties'. Together they form a unique fingerprint.

  • Cite this