Registration Dossier

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Please be aware that this old REACH registration data factsheet is no longer maintained; it remains frozen as of 19th May 2023.

The new ECHA CHEM database has been released by ECHA, and it now contains all REACH registration data. There are more details on the transition of ECHA's published data to ECHA CHEM here.

Diss Factsheets

Administrative data

Endpoint:
biochemical or cellular interactions
Type of information:
experimental study
Adequacy of study:
other information
Reliability:
2 (reliable with restrictions)
Rationale for reliability incl. deficiencies:
other: Meets generally accepted scientific standards, well documented and acceptable for assessment.

Data source

Reference
Reference Type:
publication
Title:
Inhibition of human glutathione S-transferases by basic triphenylmethane dyes.
Author:
Glanvill S.D. and Clark A.G.
Year:
1997
Bibliographic source:
Life Sciences 60 (18), 1535-1544

Materials and methods

Principles of method if other than guideline:
Human glutathione S-transferases (GSTs) of the Alpha-, Mu- and Pi- classes were expressed in E. coli and isolated by affinity chromatography. They were tested for their susceptibility to inhibition by basic triphenylmethane dyes.
GLP compliance:
no
Type of method:
in vitro

Test material

Constituent 1
Reference substance name:
Ethyl Violet
IUPAC Name:
Ethyl Violet
Details on test material:
No details.

Results and discussion

Any other information on results incl. tables

hGSTA 1-1 was inhibited by Malachite Green with a Ki value of the order of 10 microM. The inhibitory species appeared to be the dye-GSH adduct. This isoenzyme was not inhibited by either Crystal Violet or Ethyl Violet at concentrations up to 50 microM. hGSTM 2-2 was weakly inhibited by all three dyes tested with Ki values being in the range 40-80 microM. For all dyes the inhibition was best characterised as non-competitive. hGSTP 1-1 was not inhibited by Crystal Violet or by Ethyl Violet but was strongly inhibited by Malachite Green (Ki = 0.3 microM). The mode of inhibition appeared to be non-competitive but it seems probable that the mechanism is complex. There is at present no evidence to show clearly whether the dominant inhibitory species is the free dye or the adduct.

Applicant's summary and conclusion