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Purification and Characterization of Acidic Glutathione-S-Transferase from Human Peripheral Blood Leukocyte
인체 백혈구 Glutathione-S-Transferase의 정제 및 특성에 관한 연구

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Authors
Han, Jung Ho
Issue Date
1988-06
Publisher
Seoul National University College of Medicine
Citation
Seoul J Med 1988;29(2):179-186
Keywords
Glutathione-S-TransferaseHuman leuckocyteAcidic isoenzme
Abstract
An acidic isoenzyme of glutathione-S-transferase (Ee 2.5.1.18) has been purified
to homogeneity from human peripheral leukocytes through a combination of ion-exchange,
gel filtration and S-hexylglutathione-agarose affinity chromatography. The purified enzyme
exhibited specific activity of 188 ,u mol· min-1 . mg- 1 toward l-chloro-2,4-dinitrobenzene.
The molecular weight of the protein, as determined by gel filtration, was 48,000. Electrophoresis
under denaturing condition revealed a single band of molecular weight about
24500. indicating the enzyme is composed of two subunits with approximately equal size. The
enzyme had an isoelectric point of 4.6, and an apparent Km of 0.64 mM for
l-chloro-2,4-dinitrobenzene and 0.21 mM for reduced glutathione.
ISSN
0583-6802
Language
English
URI
http://hdl.handle.net/10371/6382
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Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Dept. of Medicine (의학과)The Seoul Journal of MedicineThe Seoul Journal of Medicine Vol. 29 No.2 (1988)
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