Long-term supplementation with selenate and selenomethionine: Selenium and glutathione peroxidase (EC 1.11.1.9) in blood components of New Zealand women

• Published in: British journal of nutrition 1993-03, Vol.69 (2), p.577-588
• Main Authors: Thomson, Christine D., Robinson, Marion F., Butler, Judy A., Whanger, Phllip D.
• Format: Article
• Language: English
• Subjects: Adolescent; Adult; Biological and medical sciences; Biological Availability; blood platelets; Blood Platelets - enzymology; Diet; Double-Blind Method; Effects of Selenium Supplementation; Erythrocytes - enzymology; Feeding. Feeding behavior; Female; Fundamental and applied biological sciences. Psychology; Glutathione peroxidase; Glutathione Peroxidase - blood; Humans; New Zealand; Plasma - enzymology; Platelets; Selenic Acid; Selenium; Selenium - administration & dosage; Selenium - blood; Selenium - pharmacokinetics; Selenium Compounds; Selenomethionine - administration & dosage; Selenomethionine - pharmacokinetics; Time Factors; Vertebrates: anatomy and physiology, studies on body, several organs or systems; Women
• ISSN: 0007-1145; 1475-2662
• DOI: 10.1079/BJN19930057

Thirty-three New Zealand women aged 18–23 years received daily for 32 weeks, 200 μg Se as Seenriched yeast (selenomethionine), or brewer's yeast mixed with selenate, or no added Se (placebo) in a double-blind trial. Se supplementation raised (P = 0.001), platelet glutathione peroxidase (EC 1.11.1.9; GSHPx) activity, and also Se and GSHPx in whole blood, erythrocytes and plasma. Selenomethionine was more effective in raising blood Se concentrations than selenate, but both were equally effective in raising GSHPx activities in whole blood, erythrocytes and plasma, indicating a similar bioavailability for the two forms. These observations and those of gel filtration studies of erythrocytes and plasma proteins reported elsewhere (Butler et al. 1991) are consistent with the incorporation of Se from selenomethionine into a general tissue protein pool while selenate is directly available for GSHPx synthesis, and explain the poorer correlation between Se and GSHPx in individuals with higher Se status. However, selenate raised platelet GSHPx activities to a greater extent than did selenomethionine suggesting some other effect of selenate on platelets which needs further investigation. A response of GSHPx activity in these New Zealand subjects indicates that their dietary Se intake is insufficient to meet recommended intakes based on the criterion of saturation of GSHPx activity, and could reflect a marginal Se status. The level of blood Se necessary for saturation of GSHPx of about 100 ng Se/ml whole blood confirms observations in earlier studies.