Affiliation:
1. From the Channing Laboratory and the Mallory Institute of Pathology, Boston City Hospital, and the Department of Pathology, Harvard Medical School, Boston, Massachusetts
Abstract
The role played by coenzyme Q (CoQ) in the succinic tetrazolium reductase reaction was investigated. Fresh cryostat sections of normal rat tissues were extracted with acetone to remove CoQ from the tissue sections and the acetone-extracted sections were reconstituted with CoQ-lecithin complexes. The incubation film method for tetrazolium reductases was used as a test system, using succinate as a substrate. Sections from which CoQ had been selectively extracted did not reduce the tetrazolium to its formazan, whereas those acetone-extracted sections that were treated with CoQ-lecithin complexes or with the electron carrier phenazine methosulfate reacted positively. It was concluded that the succinic tetrazolium reductase reaction requires intermediate electron carriers, mainly CoQ. It follows that nitro blue tetrazolium cannot accept electrons directly from the flavins. Therefore, the tetrazolium reductase reaction depends not only on the amount of succinic dehydrogenase and flavins but also on the amount of CoQ in the tissue.
Cited by
13 articles.
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