Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferase

Andrew P. Seddon; Marlene Bunni; Kenneth T. Douglas

doi:10.1016/0006-291X(80)90758-5

Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferase

Andrew P. Seddon
, Marlene Bunni
, Kenneth T. Douglas^*

^*Corresponding author for this work

Pharmacy

The University of Essex

Research output: Contribution to journal › Article › peer-review

Abstract

S-(p-azidophenacyl)-glutathione, l, is a linear competitive inhibitor at pH 7.40 of beef liver glyoxalase II with K_i = 7.96 × 10⁻⁴ M. On irradiation at 340 nm it covalently inhibits glyoxalase II to a level of 42 ± 5% inhibition. This photoaffinity labelling is prevented by the presence of a glyoxalase II competitive inhibitor (the hemimercaptal of glutathione and methylglyoxal). A crude preparation of sheep liver glutathione S-transferases is also irreversibly inactivated (86% ± 5% inhibition) by irradiation at 320 nm in the presence of l.

Original language	English
Pages (from-to)	446-452
Number of pages	7
Journal	Topics in Catalysis
Volume	95
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(80)90758-5
Publication status	Published - 16 Jul 1980

Access to Document

10.1016/0006-291X(80)90758-5

Cite this

@article{2725a04060694605bbed460038aafdf6,

title = "Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferase",

abstract = "S-(p-azidophenacyl)-glutathione, l, is a linear competitive inhibitor at pH 7.40 of beef liver glyoxalase II with Ki = 7.96 × 10−4 M. On irradiation at 340 nm it covalently inhibits glyoxalase II to a level of 42 ± 5\% inhibition. This photoaffinity labelling is prevented by the presence of a glyoxalase II competitive inhibitor (the hemimercaptal of glutathione and methylglyoxal). A crude preparation of sheep liver glutathione S-transferases is also irreversibly inactivated (86\% ± 5\% inhibition) by irradiation at 320 nm in the presence of l.",

author = "Seddon, \{Andrew P.\} and Marlene Bunni and Douglas, \{Kenneth T.\}",

year = "1980",

month = jul,

day = "16",

doi = "10.1016/0006-291X(80)90758-5",

language = "English",

volume = "95",

pages = "446--452",

journal = "Topics in Catalysis",

issn = "1022-5528",

publisher = "Springer Nature",

number = "1",

}

TY - JOUR

T1 - Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferase

AU - Seddon, Andrew P.

AU - Bunni, Marlene

AU - Douglas, Kenneth T.

PY - 1980/7/16

Y1 - 1980/7/16

N2 - S-(p-azidophenacyl)-glutathione, l, is a linear competitive inhibitor at pH 7.40 of beef liver glyoxalase II with Ki = 7.96 × 10−4 M. On irradiation at 340 nm it covalently inhibits glyoxalase II to a level of 42 ± 5% inhibition. This photoaffinity labelling is prevented by the presence of a glyoxalase II competitive inhibitor (the hemimercaptal of glutathione and methylglyoxal). A crude preparation of sheep liver glutathione S-transferases is also irreversibly inactivated (86% ± 5% inhibition) by irradiation at 320 nm in the presence of l.

AB - S-(p-azidophenacyl)-glutathione, l, is a linear competitive inhibitor at pH 7.40 of beef liver glyoxalase II with Ki = 7.96 × 10−4 M. On irradiation at 340 nm it covalently inhibits glyoxalase II to a level of 42 ± 5% inhibition. This photoaffinity labelling is prevented by the presence of a glyoxalase II competitive inhibitor (the hemimercaptal of glutathione and methylglyoxal). A crude preparation of sheep liver glutathione S-transferases is also irreversibly inactivated (86% ± 5% inhibition) by irradiation at 320 nm in the presence of l.

UR - https://www.scopus.com/pages/publications/0019326970

U2 - 10.1016/0006-291X(80)90758-5

DO - 10.1016/0006-291X(80)90758-5

M3 - Article

C2 - 7417267

AN - SCOPUS:0019326970

SN - 1022-5528

VL - 95

SP - 446

EP - 452

JO - Topics in Catalysis

JF - Topics in Catalysis

IS - 1

ER -

Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this