alexa Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization.
Neurology

Neurology

Journal of Clinical & Experimental Neuroimmunology

Author(s): Taguchi Y, Watanabe T, Kubota H, Hayashi H, Wada H

Abstract Share this page

Histidine decarboxylase was purified from fetal rat liver about 3,000-fold by the method described previously (Watanabe, T., Nakamura, H., Leu, Y.L., Yamatodani, A., and Wada, H. (1979) Biochem. Pharmacol. 28, 1149-1155) except that DEAE-cellulose column chromatography, Sephacryl S-300 gel filtration, and preparative polyacrylamide gel electrophoresis were added. The enzyme had a molecular weight of 110,000 in the native state and gave a single band of protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a position corresponding to a molecular weight of 54,000, indicating that it was a dimer. Its isoelectric point was pH 5.1. Antibody raised in rabbits against the enzyme gave single fused precipitation lines with the enzymes from fetal rat liver and adult rat brain and stomach in Ouchterlony's double diffusion test, and inhibited these three enzymes similarly and strongly. Using this antibody, histidine decarboxylase-like immunoreactive structures were located in fetal liver and peritoneal mast cells, stomach and brain of rats.

  • To read the full article Visit
  • Open Access
This article was published in The Journal of Biological Chemistry and referenced in Journal of Clinical & Experimental Neuroimmunology

Relevant Expert PPTs

Relevant Speaker PPTs

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords