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Department of Biochemistry, University of Nebraska College of Medicine, Omaha, Nebraska 68105
The separation of sufficient cis and trans forms of vitamin K for feeding and metabolic studies was accomplished on silica gel columns eluted with solvent containing n-butyl ether. The lack of biological activity of the cis isomer of phylloquinone was observed. The cis isomer was retained longer in liver, particularly in mitochondria, but had low retention in that portion of the endoplasmic reticulum isolated as the rough membrane fraction. The cis isomer of phylloquinone was a poor substrate for 2,3-epoxidation in vivo and in vitro. These data are consistent with the hypothesis that epoxidation of vitamin K is coupled to the biological activity of the vitamin, and that microsomes are the site of metabolism and function of vitamin K.
KEY WORDS: vitamin K cis and trans isomers epoxidation prothrombin microsomes
1 Presented to the Graduate College of the University of Nebraska in partial fulfillment of requirements for the Ph.D. degree by Thomas E. Knauer. A preliminary report of the studies contained in this paper was presented at the meeting of the American Society of Biological Chemists at Minneapolis in June 1974. These studies were supported in part by Grant HL 16912 and Contract NICHD 72-2787 from the National Institutes of Health and the Nebraska Heart Association.
2 To whom reprint requests should be sent.
Manuscript received 20 March 1975.
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