Oxidation of glycerol-3-phosphate in porcine and bovine adrenal cortex mitochondria.

• Authors: Jerzy Popinigis , Jędrzej Antosiewicz , Jan Jacek Kaczor , Hana Rauchová , Giorgio Lenaz
• Languages of publication: EN

Abstracts

EN

The capabilities of porcine adrenal cortex mitochondria to oxidize glycerol-3-phosphate (GP) were studied. In comparison with bovine adrenal cortex mitochondria, porcine mitochondria oxidized GP about three times more actively (18.9 vs 6.1 nmol O2/min per mg protein in the presence of ADP) and the activity of mitochondrial glycerol-3-phosphate dehydrogenase was about four times higher (33.4 vs 8.2 nmol/min per mg protein). In porcine adrenal cortex mitochondria we found similar values for succinate and GP oxidation both in the absence and presence of ADP or deoxycorticosterone (DOC). Rotenone sensitivity of DOC stimulation of GP oxidation indicated that porcine adrenal cortex mitochondria are able to oxidize GP and thus to generate NADPH from GP, presumably via reverse electron transport followed by energy-dependent NADH-NADP transhydrogenation.

Keywords

EN

deoxycorticosterone; glycerol-3-phosphate; adrenal cortex mitochondria; reverse electron transport; rotenone; succinate; oxidation

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2004
• Volume: 51
• Issue: 4
• Pages: 1075-1080

Dates

published

2004

received

2004-06-30

revised

2004-09-28

accepted

2004-10-20

Contributors

author

Jerzy Popinigis

• Department of Bioenergetics, Jędrzej Śniadecki University School of Physical Education and Sport, Gdańsk, Poland

author

Jędrzej Antosiewicz

• Department of Bioenergetics, Jędrzej Śniadecki University School of Physical Education and Sport, Gdańsk, Poland

author

Jan Jacek Kaczor

• Department of Bioenergetics, Jędrzej Śniadecki University School of Physical Education and Sport, Gdańsk, Poland

author

Hana Rauchová

• Institute of Physiology Academy of Sciences of the Czech Republic and Center for Cardiovascular Research, Prague, Czech Republic;

author

Giorgio Lenaz

• Department of Biochemistry "G. Morruzi", Bologna University, Bologna, Italy

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