Literature DB >> 3999920

Degradation and covalent cross-linking of glutathione reductase by hemin.

R L Aft, G C Mueller.   

Abstract

Hemin (ferriprotoporphyrin IX-chloride) can mediate the covalent cross-linking and degradation of yeast glutathione reductase. This reaction requires both NADPH and oxygen suggesting the involvement of a reduced oxygen species in the cross-linking and degradation process. During the course of the reaction the enzymatic activity of glutathione reductase is rapidly destroyed. Implications of these findings for a regulatory role of hemin in cell biology are discussed.

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Year:  1985        PMID: 3999920     DOI: 10.1016/0024-3205(85)90312-1

Source DB:  PubMed          Journal:  Life Sci        ISSN: 0024-3205            Impact factor:   5.037


  2 in total

1.  Hemin-mediated oxidation of dithiothreitol reduces oxygen to H2O.

Authors:  S Usha Devi; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1987-10       Impact factor: 3.396

Review 2.  Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.

Authors:  Doris Loh; Russel J Reiter
Journal:  Molecules       Date:  2022-01-21       Impact factor: 4.411

  2 in total

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