Literature DB >> 3345836

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

T Biswas1, F W Miller, P H Plotz.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3345836     DOI: 10.1016/0014-5793(88)80827-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Origin and regulation of a disease-specific autoantibody response. Antigenic epitopes, spectrotype stability, and isotype restriction of anti-Jo-1 autoantibodies.

Authors:  F W Miller; S A Twitty; T Biswas; P H Plotz
Journal:  J Clin Invest       Date:  1990-02       Impact factor: 14.808

2.  The role of an autoantigen, histidyl-tRNA synthetase, in the induction and maintenance of autoimmunity.

Authors:  F W Miller; K A Waite; T Biswas; P H Plotz
Journal:  Proc Natl Acad Sci U S A       Date:  1990-12       Impact factor: 11.205

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.