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Stimulation and partial stabilization of human histidyl‐tRNA synthetase by hemoglobin
Author(s) -
Biswas Tapas,
Miller Frederick W.,
Plotz Paul H.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80827-5
Subject(s) - enzyme , hemoglobin , chemistry , biochemistry , stimulation , globin , deamidation , transfer rna , microbiology and biotechnology , biology , rna , endocrinology , gene
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.