Borsook, Henry and Wasteneys, Hardolph (1925) The enzymatic synthesis of protein. II. The effect of temperature on the synthesizing action of pepsin. Journal of Biological Chemistry, 62 (3). pp. 633-639. ISSN 0021-9258 http://resolver.caltech.edu/CaltechAUTHORS:BORjbc25a
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Abstract
In a solution of the products of the hydrolysis of protein it is theoretically possible to bring about the reverse reaction, i.e. synthesis, in two ways: by concentrating the solution, and by raising the temperature. The theoretical considerations from which the first of these conclusions was deduced have been discussed in a previous paper (1). It is sufficient to recapitulate here, that the first method is predictable from an appropriate statement of the mass law. The experimental confirmation of the prediction was described by the authors (1). The second method is predictable from certain thermodynamical considerations of reversible reactions pointed out by Moore (2). He deduced the equilibrium equation Pα, = K Pnb, where Pα, and Pb, are respectively the osmotic pressures of the substrate and its product, and K is a constant. K is a symbol for the expression P0eC/RT, where P and e are constants, R is the gas constant, C is the chemical energy involved in the breakdown of 1 gram molecule of A into n gram molecules of B, and T is the absolute temperature.
| Item Type: | Article |
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| Additional Information: | © 1925 American Society for Biochemistry and Molecular Biology. Received for publication, November 1, 1924. |
| Record Number: | CaltechAUTHORS:BORjbc25a |
| Persistent URL: | http://resolver.caltech.edu/CaltechAUTHORS:BORjbc25a |
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| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. |
| ID Code: | 11653 |
| Collection: | CaltechAUTHORS |
| Deposited By: | Tony Diaz |
| Deposited On: | 19 Sep 2008 01:51 |
| Last Modified: | 26 Dec 2012 10:17 |
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