Purification of human erythrocyte transglutaminase by immunoaffinity chromatography

K. N. Lee, P. J. Birckbichler, L. Fesus

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19 Citations (Scopus)


Human erythrocyte transglutaminase was purified using a reusable immunoaffinity column prepared from a monoclonal antibody described previously (Birckbichler et al., Hybridoma, 4, 179–186, 1985). The purified TGase was catalytically active and exhibited a single band of apparent Mr=85,000 on SDS-PAGE and Western blotting. The amino acid composition of the enzyme was determined. The amino terminus was blocked, and the carboxy-terminal residue appeared to be isoleucine.

Original languageEnglish
Pages (from-to)321-335
Number of pages15
JournalPreparative Biochemistry
Issue number4
Publication statusPublished - Dec 1 1986

ASJC Scopus subject areas

  • Biochemistry
  • Genetics

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