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  • Title: Significance and redox state of SH groups in pyruvate carrier isolated from bovine heart mitochondria.
    Author: Nałecz KA, Müller M, Zambrowicz EB, Wojtczak L, Azzi A.
    Journal: Biochim Biophys Acta; 1990 Apr 05; 1016(2):272-9. PubMed ID: 2317484.
    Abstract:
    The role and properties of -SH groups of purified pyruvate (monocarboxylate) carrier were investigated. After isolation, this protein has all -SH groups in the oxidized state. Upon reduction, the carrier can be labelled with eosin-5-maleimide. The shift in apparent Mr after the labelling points to the presence of at least two cysteine residues. Pyruvate uptake in the reconstituted system is inhibited by both permeable (eosin-5-maleimide at 1 mM concentration) and impermeable (mersalyl, p-chloromercuribenzoate) -SH group reagents. Phenylarsine oxide inhibits pyruvate transport only slightly (20%), but the inhibition is enhanced after preincubation with the substrate.
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