Thiol dependent isomerization of all- trans-retinoic acid to 9- cis-retinoic acid

• Published in: FEBS letters Vol. 351; no. 3; pp. 429 - 432
• Main Authors: Urbach, Jonathan, Rando, Robert R.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 12.09.1994
• Subjects: Animals; Ascorbic Acid - metabolism; BHT, butylated hydroxytoluene; BSA, bovine serum albumin; Cattle; CMC, critical micelle concentration; DT, 1-dodecanethiol; DTT, dithiothreitol; Free Radical Scavengers; HPLC, high-pressure liquid chromatography; Isomerism; Isomerization; Microsomes, Liver - metabolism; NEM, N-ethylmaleimide; PHMB, para-hydroxymercuribenzoate; RA, all-trans-retinoic acids; Retinoid; SDS, sodium dodecyl sulfate; Sulfhydryl Compounds - metabolism; Thiol radical; Tretinoin - metabolism; Vitamin E - metabolism; DT, 1-dodecanethiol; BSA, bovine serum albumin; NEM, N-ethylmaleimide; Isomerization; Retinoid; PHMB, para-hydroxymercuribenzoate; BHT, butylated hydroxytoluene; SDS, sodium dodecyl sulfate; DTT, dithiothreitol; HPLC, high-pressure liquid chromatography; RA, all- trans-retinoic acids; CMC, critical micelle concentration; Thiol radical

The important biological effector 9- cis-retinoic acid can be generated by liver microsomes or by bovine serum albumin in detergent. The mechanism of this isomerization reaction is the subject of these studies. The protein mediated isomerization process is shown to be thiol- and pH-dependent. Moreov...