The role of adenosine-tri-phosphate in phosphate transfer from yolk to other proteins in the developing frog egg. II. Separation of the system into component enzymes, phosphate donor and phosphate acceptor
✍ Scribed by Barth, L. G. ;Jaeger, Lucena
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1950
- Tongue
- English
- Weight
- 1007 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0095-9898
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✦ Synopsis
The preceding paper h a s dealt with certain pi-operties of KC1 and NaC1 extracts of frog eggs. T h e n the proteins are precipitatcd from these extracts and incubated at pH 5.0, inorganic phosphate is liberated. Thus a phosphoprotein aiid a phosphoproteiii phospliatase are present (Harris, '46). The phosphoprotein is soon exhausted, however, and no further action takes place. Tf aa~nosiue-tri-l~hospha te ( A T P ) be added to the above proteins, Ihc observed amount of phosphate lihwated is much less than the expected arnount. This is true for the interyal during which phosphate is liberated f r o m the phosphoproteiri. After this interval the observed amount of phosphate approaches and finally exceeds the expected amount. This excess resnlts from the liberation of phosphate from ATP. The deficit in phosphate iii the presence of ATP is assumed to lw the result of a phosphate transfer from the phos-~~lioprotein to A U P and thcnce to a protciri acceptor. Evidence f o r this hypothesis has been presented in the preceding paper.
Thc purpose of the p r ~s e i i t stiidies is to separate tlic components of the almve system. A minimiim of 3 components *\iidrcl bT a grant from The Committee on G v o d h acting for The Aiiiciieaii Tancer Societr antl r2 grant from The Rockefeller Foundation.