Significance and redox state of SH groups in pyruvate carrier isolated from bovine heart mitochondria
| Autor: | Angelo Azzi, Katarzyna A. Nałȩcz, Michele Müller, Lech Wojtczak, Ewa Brygida Zambrowicz |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Monocarboxylic Acid Transporters
Pyruvate dehydrogenase kinase Pyruvate transport Biophysics In Vitro Techniques Biochemistry Redox Mitochondria Heart chemistry.chemical_compound Animals Phenylarsine oxide Sulfhydryl Compounds Pyruvates Sulfhydryl Reagents Membrane Transport Proteins Substrate (chemistry) Cell Biology Hydrogen-Ion Concentration Membrane transport Mersalyl chemistry Liposomes Cattle Carrier Proteins Oxidation-Reduction Cysteine |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1016:272-279 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/0005-2728(90)90069-g |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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