Enzymatic conversion of all-trans-. beta. -carotene to retinal by a cytosolic enzyme from rabbit and rat intestinal mucosa
- Veterans Administration Medical Center, Washington, DC (USA)
Enzymatic conversion of all-trans-{beta}-carotene to retinal by a partially purified enzyme from rabbit and rat intestinal mucosa was demonstrated. The enzymatic product was characterized based on the following evidence: (i) the product gave rise to its O-ethyloxime by treatment with O-ethylhydroxylamine with an absorption maximum at 363 nm in ethanol characteristics of authentic retinal O-ethyloxime. High-pressure liquid chromatography (HPLC) of this derivative yielded a sharp peak with a retention time of 7.99 min corresponding to the authentic compound; (ii) the mass spectrum of the O-ethyloxime of the enzymatic product was identical to that of authentic retinal O-ethyloxime; (iii) the specific activity of the enzymatically formed ({sup 14}C)retinal O-ethyloxime remained constant even after repeated crystallization; (iv) the enzymatic product exhibited an absorption maximum at 370 nm in light petroleum characteristic of authentic retinal. This retinol was enzymatically esterified to retinyl palmitate by rat pancreatic esterase with a retention time of 10 min on HPLC corresponding to authentic retinyl palmitate. Thus, the enzymatic product of {beta}-carotene cleavage by the partially purified intestinal enzyme was unequivocally confirmed to be retinal.
- OSTI ID:
- 7138120
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 86:23; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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LIQUID COLUMN CHROMATOGRAPHY
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550201* - Biochemistry- Tracer Techniques