scholarly journals Glutathione S-aralkyltransferase

1969 ◽  
Vol 115 (5) ◽  
pp. 985-991 ◽  
Author(s):  
E. Boyland ◽  
L. F. Chasseaud
Keyword(s):  
Ammonium Sulphate ◽  
Rat Liver ◽  
Benzyl Chloride ◽  
Animal Species ◽  
Rat Kidney ◽  
Acid Precipitation ◽  
Heat Inactivation ◽  
Catalysed Reaction ◽  
Glutathione S Transferases ◽  
Ammonium Sulphate Fractionation

1. The name ‘glutathione S-aralkyltransferase’ is proposed for the enzyme catalysing the reaction of benzyl chloride with GSH. 2. Results from heat-inactivation studies, ammonium sulphate-fractionation and acid-precipitation experiments, and studies of the distribution of activities in rat liver, in rat kidney and in the livers of other animals indicate that glutathione S-aralkyltransferase differs from glutathione S-alkyltransferase, S-aryltransferase, S-epoxidetransferase and an S-alkenetransferase. 3. The distribution of these enzymes in the livers of the animal species examined was different. 4. Glutathione S-alkyltransferase, S-aralkyltransferase and the S-alkenetransferase that are present in rat liver supernatant were inhibited by GSSG, and the nature of the inhibition varied in each case. 5. 3,5-Di-tert.-butyl-4-hydroxybenzyl acetate reacts spontaneously with GSH, but the rat liver-supernatant-catalysed reaction of GSH with this and other aralkyl esters was weak. 6. A probable function of the glutathione S-transferases is the protection of cellular constituents from strong electrophilic agents.

scholarly journals Enzymes catalysing conjugations of glutathione with αβ-unsaturated carbonyl compounds

1968 ◽  
Vol 109 (4) ◽  
pp. 651-661 ◽  
Author(s):  
E. Boyland ◽  
L. F. Chasseaud
Keyword(s):  
Ammonium Sulphate ◽  
Carbonyl Compounds ◽  
Lower Energy ◽  
Rat Kidney ◽  
Heat Inactivation ◽  
Phenoxyacetic Acid ◽  
Diethyl Maleate ◽  
Catalysed Reaction ◽  
Ammonium Sulphate Fractionation ◽  
Inhibition Studies

1. Heat-inactivation experiments, ammonium sulphate-fractionation studies, enzyme-inhibition studies with S-(αβ-diethoxycarbonylethyl)glutathione, and evidence from the distribution of activities in rat liver, in rat kidney and in the livers of other animals, indicate that reactions of glutathione with (i) trans-benzylideneacetone, (ii) cyclohex-2-en-1-one, (iii) trans-cinnamaldehyde, (iv) diethyl maleate, (v) diethyl fumarate and (vi) 2,3-dimethyl-4-(2-methylenebutyryl)phenoxyacetic acid are catalysed by different enzymes. 2. Evidence is presented that the enzymes catalysing the reactions of glutathione with substrates (i)–(iv) are different from glutathione S-alkyltransferase, S-aryltransferase and S-epoxidetransferase. 3. The name ‘glutathione S-alkenetransferases’ is proposed for enzymes catalysing reactions of glutathione with αβ-unsaturated compounds. 4. The Arrenhius plot for the enzyme-catalysed reaction of diethyl maleate with glutathione is discontinuous, with lower energy of activation at 38°.

scholarly journals Distribution of enzymes that catalyse reactions of glutathione with αβ-unsaturated compounds

1973 ◽  
Vol 131 (4) ◽  
pp. 765-769 ◽  
Author(s):  
L. F. Chasseaud
Keyword(s):  
Guinea Pig ◽  
Rat Liver ◽  
Rat Kidney ◽  
Acid Precipitation ◽  
Heat Inactivation ◽  
Phenoxyacetic Acid ◽  
Mercapturic Acids ◽  
Vertebrate Species ◽  
Methyl Vinyl

1. A study of the distribution of glutathione S-alkenetransferases in the livers of vertebrate species suggests that different enzymes may catalyse reactions of GSH with (i) trans-benzylideneacetone, (ii) 2,3-dimethyl-4(2-methylenebutyryl)phenoxyacetic acid, (iii) cinnamonitrile, (iv) o-chlorobenzylidenemalononitrile, (v) methyl vinyl sulphone, and (vi) 3-(β-nitrovinyl)indole. 2. Glutathione S-alkenetransferase activity was generally greatest in rat liver, but the enzyme in hamster liver was more active towards o-chlorobenzylidenemalononitrile, and the enzyme in rabbit, hamster, guinea-pig and mouse livers was more active towards methyl vinyl sulphone. 3. Results from studies of the distribution of activities in rat liver and rat kidney, heat inactivation of rat liver supernatants, and (NH4)2SO4 fractionation and acid-precipitation experiments, differentiated further between some of the enzymes concerned with substrates (i)–(vi). 4. The infrequent detection of mercapturic acids in vivo is discussed.

GLYCYL-RNA SYNTHETASE OF RAT LIVER: PARTIAL PURIFICATION AND EFFECTS OF SOME METAL IONS ON ITS ACTIVITY

1963 ◽  
Vol 41 (1) ◽  
pp. 1123-1133 ◽  
Author(s):  
M. J. Fraser
Keyword(s):  
Heat Treatment ◽  
Metal Ions ◽  
Ammonium Sulphate ◽  
Rat Liver ◽  
Partial Purification ◽  
Ammonium Sulphate Fractionation ◽  
Stimulation Of

Glycyl-RNA synthetase has been purified 40-fold from a 105,000 × g supernatant of an homogenate of rat liver by successive precipitation at pH = 5.0, heat treatment at 55 °C for 3.0 minutes in the presence of 1.0 mM ATP, and ammonium sulphate fractionation. The purified fractions catalyzed glycine-dependent ATP-32PP exchange. The effect of some metal ions on glycine activation was studied. Activation occurred in the presence of either Mg++or Mn++. The apparent stimulation of glycine activation by Co++was found to be an artifact.

scholarly journals Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations

1996 ◽  
Vol 314 (3) ◽  
pp. 1017-1025 ◽  
Author(s):  
Horng-I. YEH ◽  
Jing-Yu LEE ◽  
Shu-Ping TSAI ◽  
Cheng-Hsilin HSIEH ◽  
Ming F. TAM
Keyword(s):  
Rat Liver ◽  
Peptide Mapping ◽  
Rat Kidney ◽  
Cdna Sequencing ◽  
Sequencing Data ◽  
Glutathione S Transferase ◽  
Reverse Phase Hplc ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Molecular Masses

Cytosolic glutathione S-transferases (GSTs) from rat kidneys were purified by a combination of glutathione and S-hexylglutathione affinity columns. The isolated GSTs were subjected to reverse-phase HPLC and electrospray MS analysis. The major GST isoenzymes expressed in kidney are subunits 1, 2, 7 and 8. GST 1´, 3, and 4 are expressed in minor amounts. GST 10 is barely detectable in the male kidney cytosol. The molecular masses of these rat kidney GST subunits were determined by MS. The values obtained for subunits 1´, 2, 3, 4, 7, 8 and 10 are identical with those obtained for rat liver GSTs. Rat kidney GST 1 consists of three polypeptides, with molecular masses of 25517, 25372 and 24982 Da. Results from peptide mapping, MS and amino-acid-sequencing analyses indicate that the major components were generated by deleting the C-terminal phenylalanine (24982 Da) and the C-terminal IFKF tetrapeptide (25372 Da) from the GST 1 subunit, respectively. The 1-chloro-2,4-dinitrobenzene-conjugating and peroxidase activities of kidney GST 1 are substantially lower than for its counterpart from rat liver. In addition, rat kidney GST 1 has an arginine and a valine residue at positions 151 and 207 respectively. The results are in contradiction with the SWISS-PROT and GenBank rat liver GST 1 cDNA-sequencing data, which give a lysine and a methionine at the corresponding positions. Further analyses indicate that rat liver GST 1 also has C-terminal phenylalanine deletion, and an arginine and a valine residue at positions 151 and 207 respectively. However, the C-terminal-tetrapeptide-deleted form was not observed for rat liver GST 1.

GLYCYL-RNA SYNTHETASE OF RAT LIVER: PARTIAL PURIFICATION AND EFFECTS OF SOME METAL IONS ON ITS ACTIVITY

1963 ◽  
Vol 41 (5) ◽  
pp. 1123-1133 ◽  
Author(s):  
M. J. Fraser
Keyword(s):  
Heat Treatment ◽  
Metal Ions ◽  
Ammonium Sulphate ◽  
Rat Liver ◽  
Partial Purification ◽  
Ammonium Sulphate Fractionation ◽  
Stimulation Of

Glycyl-RNA synthetase has been purified 40-fold from a 105,000 × g supernatant of an homogenate of rat liver by successive precipitation at pH = 5.0, heat treatment at 55 °C for 3.0 minutes in the presence of 1.0 mM ATP, and ammonium sulphate fractionation. The purified fractions catalyzed glycine-dependent ATP-32PP exchange. The effect of some metal ions on glycine activation was studied. Activation occurred in the presence of either Mg++or Mn++. The apparent stimulation of glycine activation by Co++was found to be an artifact.

scholarly journals Canine submandibular-gland hyaluronidase. Purification and properties

1968 ◽  
Vol 110 (1) ◽  
pp. 19-25 ◽  
Author(s):  
Y. H. Tan ◽  
J. M. Bowness
Keyword(s):  
Submandibular Gland ◽  
Ammonium Sulphate ◽  
Rat Liver ◽  
Gel Filtration ◽  
Acid Precipitation ◽  
Ammonium Sulphate Precipitation ◽  
Purification And Properties ◽  
Freeze Dried ◽  
Specific Activities

1. Methods for the purification of dog submandibular-gland hyaluronidase from sedimentable and non-sedimentable portions of a homogenate and from the whole homogenate are presented. The method consists of three main steps: removal of mucin by acid precipitation or gel filtration on Sephadex G-200, ammonium sulphate precipitation and CM-cellulose chromatography. By this method specific activities of up to 1·28 and 0·78μmoles of N-acetylglucosamine/min./mg. of protein were obtained for the purified freeze-dried non-sedimentable hyaluronidase and for the sedimentable hyaluronidase respectively. 2. A comparison of some of the properties of the non-sedimentable and the sedimentable hyaluronidase preparation indicated that there was little difference between the two and that they both resembled lysosomal hyaluronidase from rat liver.

scholarly journals Studies on the subunit composition of rat liver glutathione S-transferases.

1983 ◽  
Vol 258 (18) ◽  
pp. 11321-11325 ◽  
Author(s):  
A B Frey ◽  
T Friedberg ◽  
F Oesch ◽  
G Kreibich
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases
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