Literature DB >> 3985982

A rapid, novel high performance liquid chromatography method for the purification of glutathione S-transferase: an application to the human placental enzyme.

L L Radulovic, A P Kulkarni.   

Abstract

A simple High Performance Liquid Chromatography procedure is detailed for the purification of Glutathione S-transferase. The human placental transferase was used to assess its potential. Unlike conventional methods of purification, the procedure is rapid and resolution of the various forms is achieved in less than 20 min. Since recovery is essentially complete, it is possible to isolate different minor forms. Three forms, one major and two minor, were separated. The major form represented about 97% of the total recovered activity and exhibited a specific activity of 254.94 mumoles/min/mg protein with a purification of 1342-fold. Electrophoresis of the major form revealed the presence of a single band, suggesting homogeneity.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3985982     DOI: 10.1016/0006-291x(85)91646-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  H.p.l.c. separation and study of the charge isomers of human placental glutathione transferase.

Authors:  L L Radulovic; A P Kulkarni
Journal:  Biochem J       Date:  1986-10-01       Impact factor: 3.857

2.  Inhibition of cell proliferation and glutathione S-transferase by ascorbyl esters and interferon in mouse glioma.

Authors:  A K Naidu; M Wiranowska; S H Kori; K C Roetzheim; A P Kulkarni
Journal:  J Neurooncol       Date:  1993-04       Impact factor: 4.130

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.