Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 30, Issue 3, Pages 327-333Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0891-5849(00)00483-4
Keywords
human serum albumin; peroxidase activity; palmitoyl coenzyme A; thioredoxin; free radicals
Ask authors/readers for more resources
Human Serum Albumin (HSA) exerted a significant lipid peroxidase activity with the use of a thiol-reducing equivalent such as dithiothreitol (DTT). Carboxyl group-modified HSA (CM-HSA) showed a 10-fold stronger lipid peroxidase activity (1.6 nmol/min/mg) than that of HSA (0.17 nmol/min/mg). Instead of DTT, thioredoxin (Trx) also supported reducing equivalent to the reduction of lipid hydroperoxide by CM-HSA. Contrast to CM-HSA, HSA did not reduce lipid pet-oxide with the use of Trx. In the presence of palmitoyl coenzyme A (palmitoyl-CoA) however, HSA used Trx as an electron donor to the reduction of lipid hydroperoxide. The Trx-linked peroxidase activity of HSA sharply increased with elongation in the carbon chain of the acyl moiety of acyl-CoA, showing an optimum activity in the presence of palmitoyl-CoA Fluorescence study indicates the conformational changes of HSA induced by palmitoyl-CoA, Together, these data suggest that palmitoyl-CoA-bound HSA has a capability to remove lipid peroxide with the use of electrons given by Trx system. (C) 2001 Elsevier Science Inc.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available