Stimulation and partial stabilization of human histidyl-tRNA synthetase by hemoglobin

Tapas Biswas, Frederick W. Miller, Paul H. Plotz

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Histidyl-tRNA synthetase, an enzyme against which antibodies are directed in some patients with polymyositis, has been purified 5000-fold from HeLa cells, but was extremely labile to dilution or on storage at -80°C. In order to facilitate study of the biochemical and immunological properties of the enzyme, a stabilizer was sought. Hemoglobin at 2 mg/ml was found to stimulate the enzyme and also partially preserved the activity of the enzyme stored at a low concentration (<10μg/ml). Hematin, but not the globin protein, could substitute for hemoglobin in stimulating the enzyme.

Original languageEnglish (US)
Pages (from-to)203-205
Number of pages3
JournalFEBS Letters
Issue number1
StatePublished - Feb 29 1988
Externally publishedYes


  • Autoantigen
  • Hematin
  • Hemoglobin stabilization
  • Histidyl-tRNA synthetase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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