Stimulation and partial stabilization of human histidyl-tRNA synthetase by hemoglobin.
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 degrees 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 (less than 10 micrograms/ml). Hematin, but not the globin protein, could substitute for hemoglobin in stimulating the enzyme.
Biswas
T
T
Arthritis and Rheumatism Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Bethesda, MD 20892.
Miller
F W
FW
Plotz
P H
PH
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001323:Autoantibodies; D006367:HeLa Cells / Q000201:enzymology; D006454:Hemoglobins / Q000378:metabolism*; D006643:Histidine-tRNA Ligase / Q000378:metabolism*; D006801:Humans; D009220:Myositis / Q000201:enzymology / Q000276:immunology
D001323:Autoantibodies; D006454:Hemoglobins; D000604:Amino Acyl-tRNA Synthetases; D006643:Histidine-tRNA Ligase