1. Rapid incorporation of P
32-cocarboxylase into the terminal P of ATP was observed in the tissue homogenate or especially in the liver cyclophorase system in the presence of α-ketoglutarate or pyruvate.
2. From the experiment using the liver cyclophorase system it was especially indicated that there might be a direct route (not via inorganic P) of phosphate transfer from cocarboxylase to the terminal P of ATP in the presence of α-ketoglutarate or pyruvate.
3. A mechanism assuming that a binding form of cocarboxylase (lipothiamide pyrophosphate) might be formed as an intermediate, may be forwarded from the study in which various amounts of cocarboxylase was incubated with cyclophorase system in the presence of α-ketoglutar-ate.
4. Approximate rate of the incorporation of P
32 of P
32-cocarboxylase into ATP was compared with that of inorganic P
32 in the presence of NaF which prevented almost completely the release of inorganic P from cocarboxylase.
5. The rate of the incorporation of P
32-cocarboxylase into ATP was not inhibited by 2, 4-dinitrophenol.
6. The added cocarboxylase appeared as labile P in the liver cyclophorase system.
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