Sulfhydryl groups and transketolase activity.
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Extracts of pigeon liver acetone powder showed, by a radiochemical method, considerable pyruvate decarboxylating activity. The 10-30% saturated ammonium sulfate fraction of these extracts required the addition of CoA, NAD+, and TPP for maximum pyruvate decarboxylating activity and presumably contained the pyruvate dehydrogenase complex (PDHC). The activity in the 40-60% saturated ammonium sulfate fraction had no requirement for CoA and/or NAD+ but had an absolute requirement for TPP. In similar preparations obtained from fresh pigeon liver, the PDHC activity was found in the 0-30% saturated ammonium sulfate fraction and only a small amount of pyruvate decarboxylating activity (independent of CoA and NAD+) was found in the 40-60% saturated ammonium sulfate fraction. The pyruvate decarboxylating activity which is found in the 40-60% saturated ammonium sulfate fraction of these extracts and has an absolute requirement for TPP, may represent pyruvate dehydrogenase (E1, EC 1.2.4.1), probably derived from PDHC by the acetone treatment at pH 7.8, or aging of the preparation.
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