Purification of aldehyde oxidase from bovine ciliary body.

Abstract:

:Ocular aldehyde oxidase was purified for the first time from bovine ciliary body cytosol by ammonium sulfate fractionation and successive HPLC using DEAE anion-exchange and hydroxyapatite columns. The purified enzyme was homogeneous by the criterion of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 150,000 by electrophoresis and to be about 300,000 by gel filtration HPLC on a TSK gel G3000SWXL column, indicating that the enzyme consists of two subunits with the same molecular weight. On the other hand, nicotinamide N-oxide reductase activity was associated with aldehyde oxidase activity throughout the purification steps of the latter enzyme. This fact indicated that nicotinamide N-oxide reductase activity of the ciliary body cytosol is due to aldehyde oxidase present in the tissue preparation.

journal_name

Curr Eye Res

journal_title

Current eye research

authors

Shimada S,Mishima HK,Nikaido H,Kitamura S,Tatsumi K

doi

10.3109/02713688909025807

subject

Has Abstract

pub_date

1989-07-01 00:00:00

pages

721-6

issue

7

eissn

0271-3683

issn

1460-2202

journal_volume

8

pub_type

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