Purification of glycineamide ribonucleotide transformylase

C. A. Caperelli, G. Chettur, L. Y. Lin, S. J. Benkovic

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17 Scopus citations


Glycineamide ribonucleotide transformylase has been purified 240-fold from chicken liver along with formyl-methenyl-methylenetetrahydrofolate synthetase (combined), through seven purification steps including a glycineamide ribonucleotide affinity column and a 10-formyl synthetase specific MgATP elution from hydroxylapatite. The transformylase is a homodimer of Mr 63,000 whereas the synthetase (combined) is composed of two identical subunits of Mr 83,000. Transformylase has been isolated free of the synthetase (combined) by an additional anion exchange chromatographic step resulting in a net 400-fold purification.

Original languageEnglish (US)
Pages (from-to)403-410
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - May 30 1978

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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