M
Michael J. Pabst
Researcher at National Institutes of Health
Publications - 6
Citations - 17921
Michael J. Pabst is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Glutathione & Transferase. The author has an hindex of 5, co-authored 6 publications receiving 16683 citations.
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Journal ArticleDOI
Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.
TL;DR: The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related.
Journal ArticleDOI
The identity of glutathione S-transferase B with ligandin, a major binding protein of liver.
William H. Habig,Michael J. Pabst,G Fleischner,Zenaida Gatmaitan,Irwin M. Arias,William B. Jakoby +5 more
TL;DR: Evidence is presented that ligandin, an intracellular protein involved in the binding of such anions as bilirubin, indocyanine green, and penicillin, is identical to glutathione S-transferase B, and it is suggested that specificity is directed toward compounds with electrophilic sites.
Journal ArticleDOI
Glutathione S-transferase A. A novel kinetic mechanism in which the major reaction pathway depends on substrate concentration.
TL;DR: Initial velocity, product inhibition, and binding studies indicate a biphasic kinetic mechanism in which the reaction pathway depends on the concentration of the substrates, and a numerical rate equation was developed which describes initial velocities over the entire range of substrate concentrations.
Journal ArticleDOI
Glutathione S-transferase AA from rat liver
TL;DR: The catalytic properties of transfer enzyme AA are very similar to those of transferase B although the two proteins differ in their ability to bind bilirubin and other ligands, in their amino acid composition, and in their immunological properties.
Journal ArticleDOI
Mercapturic acid formation: The several glutathione transferases of rat liver
TL;DR: Although there are differences in specificity among the enzyme species, such differences are not directly related to the nucleophilic leaving group and it is not accurate to classify the enzymes by their preferences for substrates of a particular type of hydrocarbon skeleton.