Identification and immunohistochemistry of retinol dehydrogenase from bovine retinal pigment epithelium.

Y Suzuki, S Ishiguro, M Tamai

Department of Ophthalmology, Tohoku University School of Medicine, Sendai, Japan.

Biochimica et biophysica acta 1993 May 13

filter terms:

We studied the properties of retinol dehydrogenase (11-cis-specific) from bovine retinal pigment epithelium. Detergents caused a loss of retinol dehydrogenase activity; therefore, we added 3 mM NADH as a stabilizer to solubilize this enzyme and partially purified this enzyme using Sepharose CL-6B and hydroxyapatite column chromatography. The partially-purified sample, which contained two major proteins (66 kDa, 33 kDa), had substrate preference to 11-cis and 13-cis-retinal but not to all-trans and 9-cis isomers. Monoclonal anti-33 kDa protein of retinal pigment epithelial crude extract by Western blotting. In addition, we found that monoclonal anti-retinol dehydrogenase anti body bound specifically to retinal pigment epithelium and not to Müller cells or to rod outer segments by immunohistochemical methods.

Citation

Y Suzuki, S Ishiguro, M Tamai. Identification and immunohistochemistry of retinol dehydrogenase from bovine retinal pigment epithelium. Biochimica et biophysica acta. 1993 May 13;1163(2):201-8