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No enzymatic activities are necessary for the stabilization of ascorbic acid by K‐562 cells
Author(s) -
Schweinzer Esther,
Waeg Georg,
Esterbauer Hermann,
Goldenberg Hans
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81691-r
Subject(s) - ascorbic acid , enzyme , chemistry , chelation , substrate (aquarium) , biochemistry , membrane , reductase , substrate specificity , biology , organic chemistry , food science , ecology
We disprove that living cells stabilize ascorbate by the activity of a trans plasma membrane semidehydroascorbate reductase. The two processes show different specificities for both substrate and inhibitor. Not only cells but also cell‐conditioned buffers stabilize ascorbate as long as compounds with molecular weights above 10 kDa are not removed. The effect is most probably due to chelation of traces of transition metals.