Characterization of glutathione S-transferases of human cornea

Shivendra V. Singh, Thomas D. Hong, Satish Srivastava, Yogesh C. Awasthi

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22 Scopus citations

Abstract

Two cationic (pIs 9·1 and 7·6) and one anionic (pI 4·4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.

Original languageEnglish (US)
Pages (from-to)431-437
Number of pages7
JournalExperimental Eye Research
Volume40
Issue number3
DOIs
StatePublished - 1985

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Keywords

  • detoxication
  • glutathione peroxidase II
  • glutathione S-transferases
  • human cornea

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Singh, S. V., Hong, T. D., Srivastava, S., & Awasthi, Y. C. (1985). Characterization of glutathione S-transferases of human cornea. Experimental Eye Research, 40(3), 431-437. https://doi.org/10.1016/0014-4835(85)90155-1