Aldose reductase has been purified to homogeneity from bovine retina. It has an apparent molecular weight of 32,000 daltons and shares immunological and kinetic properties with the much studied aldose reductases purified from various sources. Retinal aldose reductase displays a K(m) of approximately 40 μM with 4-hydroxynonenal and 4-hydroxyhexenal, the oxidation end products of arachidonic and docosahexanoeic acids, respectively. It therefore appears that aldose reductase may constitute a major detoxification route of these toxic aldehydes in the retina.
|Original language||English (US)|
|Number of pages||4|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jun 29 1998|
Bibliographical noteFunding Information:
This study was partially supported by NIH Grant EY 08547, the Lions Eye Bank Foundation, and Texas Higher Education. The authors thank Ms. Terry Campbell for typing the manuscript.