Calcium-dependent affinity purification of transclutaminase from rat liver cytosol

Dorothy E. Croall, George N. DeMartino

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Tissue transglutaminase (E.C., R-glutaminyl-peptide: amine glutaminyl transferase), was purified from extracts of rat liver by calcium dependent affinity chromatography on casein-Sepharose. In the presence of 5mM calcium the enzyme binds to casein Sepharose and is subsequently eluted with 5mM EGTA. The enzyme has a molecular weight of 83,000 and its activity is dependent on calcium and reduced sulfhydryl residues. A widely distributed calcium-dependent protease (E.C. copurified with transglutaminase by gel filtration and ion exchange chromatography. The separation of these activities prior to chromatography on casein-Sepharose is essential for the isolation of a stable transglutaminase by calcium-dependent affinity chromatography. Affinity chromatography using casein-Sepharose or other immobilized substrates may allow the calcium-dependent purification of a variety of transglutaminases.

Original languageEnglish (US)
Pages (from-to)29-39
Number of pages11
JournalCell Calcium
Issue number1
StatePublished - Feb 1986

ASJC Scopus subject areas

  • Physiology
  • Molecular Biology
  • Cell Biology


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