I t has been shown by isotope techniques (Rothstein and AIeier, '48) that a number of acid phosphatases are located on the cell surface of yeast. These phosphatases can hydrolyze such substrates as adenosine triphosphate, adenosine diphosphat e, inorganic t riphosphat e and pyrophosphat e, phenyl pl
The relationship of the cell surface to metabolism. I. Phosphatases in the cell surface of living yeast cells
โ Scribed by Rothstein, Aser ;Meier, Rebecca
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1948
- Tongue
- English
- Weight
- 804 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0095-9898
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โฆ Synopsis
In the conrse of experiments with liviiig yeast cells, it mas found tliat adenmine triyliosphate (ATP) added to the mecliuin was hydrolyzed to inorganic phosphate plus aderiylic acid. Tlie quantitative recovery of the 1woclncts of lipclrolysis in the inediuxn suggested tliat the phospliate-splittiii~ erizynie or enzymes inight be in the surface rather than in the interior of thc cells. I n this connection, it has recently been sliowii by cytocheniical tecbiiiqnes that various phospliatases are present in iiitestiiie aiid kidney, riot o d y ill tlie interior of the cell and in the ~iucleus, hilt in the outermost zone of the cytoplasin adjacent to the cell surface, a s mcll (Deinpsey and Dean, '46 and Emnel, '46). The cspcriiiiexits reported here involve the use of isotopic phosphorus ( PS2) to clenioiistratc chemically that the splitting of adenosine triphospliate by living yeast takes place 011 the surface of tlie cell; certain cliaracteristics of the enzyme h a r e been determined i n sitzr, that is, in the liriiig cell; and the esistence on the surface of other pli o splia t e-spli t t iiig en zynie s h a s be en demon s t r a t ed.
This document is based on the woik yerforinrd iinder Contra( t JV-7401-eng-49 for the Stomie Energj Project a t the Uiiiversit? of Roclicstei.
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## FOUR FIGURES I n previous papers of this series (Rothstein and Larrabee, '48 ; Rothstein, Frenkel and Larrabee, '48 ; Rothstein, Rleier and Hurwitz, '51; Rothstein and Meier, '51), it has been shown that the uranyl ion specifically inhibits the metabolism of hexoses by forming a highly undissoc