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Identification of polymorphism at the glutathione S-transferase, GSTM3 locus: evidence for linkage with GSTM1 * A

A Inskip, J Elexperu-Camiruaga, N Buxton, P S Dias, J MacIntosh, D Campbell, P W Jones, L Yengi, J A Talbot, R C Strange, A A Fryer

Biochem J (1995) 312 (3): 713–716.

https://doi.org/10.1042/bj3120713

Published: 15 December 1995

View article titled, Identification of polymorphism at the glutathione S-transferase, GSTM3 locus: evidence for linkage with GSTM1 * A

Articles

Use of site-directed mutagenesis of allele-specific PCR primers to identify the GSTM1 A, GSTM1 B, GSTM1 A,B and GSTM1 null polymorphisms at the glutathione S-transferase, GSTM 1 locus

A A Fryer, L Zhao, J Alldersea, W R Pearson, R C Strange

Biochem J (1993) 295 (1): 313–315.

https://doi.org/10.1042/bj2950313

Published: 01 October 1993

View article titled, Use of site-directed mutagenesis of allele-specific PCR primers to identify the GSTM1 A, GSTM1 B, GSTM1 A,B and GSTM1 null polymorphisms at the glutathione S-transferase, GSTM 1 locus

Articles

The human glutathione S -transferases. Immunohistochemical studies of the developmental expression of Alpha- and Pi-class isoenzymes in liver

C Hiley, A Fryer, J Bell, R Hume, R C Strange

Biochem J (1988) 254 (1): 255–259.

https://doi.org/10.1042/bj2540255

Published: 15 August 1988

View article titled, The human glutathione S -transferases. Immunohistochemical studies of the developmental expression of Alpha- and Pi-class isoenzymes in liver

Articles

Studies of the development of basic, neutral and acidic isoenzymes of glutathione S -transferase in human liver, adrenal, kidney and spleen

C G Faulder, P A Hirrell, R Hume, R C Strange

Biochem J (1987) 241 (1): 221–228.

https://doi.org/10.1042/bj2410221

Published: 01 January 1987

View article titled, Studies of the development of basic, neutral and acidic isoenzymes of glutathione S -transferase in human liver, adrenal, kidney and spleen

Articles

Erythrocyte glutathione S -transferase. Electrophoretic identification of two enzyme forms

R C Strange, P H Hirrell, G A Kitley, D A Hopkinson, W Cotton

Biochem J (1983) 215 (1): 213–216.

https://doi.org/10.1042/bj2150213

Published: 01 October 1983

View article titled, Erythrocyte glutathione S -transferase. Electrophoretic identification of two enzyme forms

Articles

A study of the structures of the YaYa and YaYc glutathione S -transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activity

J D Hayes, R C Strange, I W Percy-Robb

Biochem J (1981) 197 (2): 491–502.

https://doi.org/10.1042/bj1970491

Published: 01 August 1981

View article titled, A study of the structures of the YaYa and YaYc glutathione S -transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activity

Articles

A comparison of erythrocyte glutathione S -transferase activity from human foetuses and adults

R C Strange, J D Johnston, D R Coghill, R Hume

Biochem J (1980) 188 (2): 475–479.

https://doi.org/10.1042/bj1880475

Published: 15 May 1980

View article titled, A comparison of erythrocyte glutathione S -transferase activity from human foetuses and adults

Articles

Cholic acid binding by glutathione S -transferases from rat liver cytosol

J D Hayes, R C Strange, I W Percy-Robb

Biochem J (1980) 185 (1): 83–87.

https://doi.org/10.1042/bj1850083

Published: 01 January 1980

View article titled, Cholic acid binding by glutathione S -transferases from rat liver cytosol

Articles

Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S -transferase B

J D Hayes, R C Strange, I W Percy-Robb

Biochem J (1979) 181 (3): 699–708.

https://doi.org/10.1042/bj1810699

Published: 01 September 1979

View article titled, Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S -transferase B

Articles

Nuclear and cytosolic distribution of conjugated cholic acid and radiolabelled glycocholic acid in rat liver

R C Strange, G J Beckett, I W Percy-Robb

Biochem J (1979) 178 (1): 71–78.

https://doi.org/10.1042/bj1780071

Published: 15 January 1979

View article titled, Nuclear and cytosolic distribution of conjugated cholic acid and radiolabelled glycocholic acid in rat liver

Articles

Partial purification of two lithocholic acid-binding proteins from rat liver 100000 g supernatants

R C Strange, R Cramb, J D Hayes, I W Percy-Robb

Biochem J (1977) 165 (3): 425–429.

https://doi.org/10.1042/bj1650425

Published: 01 September 1977

View article titled, Partial purification of two lithocholic acid-binding proteins from rat liver 100000 g supernatants

Articles

An evaluation of ways of using equilibrium dialysis to quantify the binding of ligand to macromolecule

I A Nimmo, G L Atkins, R C Strange, I W Percy-Robb

Biochem J (1977) 165 (1): 107–110.

https://doi.org/10.1042/bj1650107

Published: 01 July 1977

View article titled, An evaluation of ways of using equilibrium dialysis to quantify the binding of ligand to macromolecule

Articles

Binding of bile acids by 100 000 g supernatants from rat liver

R C Strange, I A Nimmo, I W Percy-Robb

Biochem J (1977) 162 (3): 659–664.

https://doi.org/10.1042/bj1620659

Published: 15 March 1977

View article titled, Binding of bile acids by 100 000 g supernatants from rat liver

Articles

Equilibrium-dialysis studies of the interaction between cholic acid and 100000 g -supernatant preparations from the rat liver

R C Strange, I A Nimmo, I W Percy-Robb

Biochem J (1976) 156 (2): 427–433.

https://doi.org/10.1042/bj1560427

Published: 15 May 1976

View article titled, Equilibrium-dialysis studies of the interaction between cholic acid and 100000 g -supernatant preparations from the rat liver

Articles

Hepatic clearance of adenosine 3′:5′-cyclic monophosphate from plasma in the rat

R C Strange, I W P Robb

Biochem J (1975) 146 (2): 509–512.

https://doi.org/10.1042/bj1460509

Published: 15 February 1975

View article titled, Hepatic clearance of adenosine 3′:5′-cyclic monophosphate from plasma in the rat

NARROW

Identification of polymorphism at the glutathione S-transferase, GSTM3 locus: evidence for linkage with GSTM1 * A

Use of site-directed mutagenesis of allele-specific PCR primers to identify the GSTM1 A, GSTM1 B, GSTM1 A,B and GSTM1 null polymorphisms at the glutathione S-transferase, GSTM 1 locus

The human glutathione S -transferases. Immunohistochemical studies of the developmental expression of Alpha- and Pi-class isoenzymes in liver

Studies of the development of basic, neutral and acidic isoenzymes of glutathione S -transferase in human liver, adrenal, kidney and spleen

Erythrocyte glutathione S -transferase. Electrophoretic identification of two enzyme forms

A study of the structures of the YaYa and YaYc glutathione S -transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activity

A comparison of erythrocyte glutathione S -transferase activity from human foetuses and adults

Cholic acid binding by glutathione S -transferases from rat liver cytosol

Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S -transferase B

Nuclear and cytosolic distribution of conjugated cholic acid and radiolabelled glycocholic acid in rat liver

Partial purification of two lithocholic acid-binding proteins from rat liver 100000 g supernatants

An evaluation of ways of using equilibrium dialysis to quantify the binding of ligand to macromolecule

Binding of bile acids by 100 000 g supernatants from rat liver

Equilibrium-dialysis studies of the interaction between cholic acid and 100000 g -supernatant preparations from the rat liver

Hepatic clearance of adenosine 3′:5′-cyclic monophosphate from plasma in the rat

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