196 OXIDATION-REDUCTION POTENTIALS 



Shaffer, P. A. (1936). Catalysis of ionic oxidation-reduction reactions by dyes and its probable 

 mechanism. J. Physiol. Chew,., 40, 1021. 



and Williams, R. D. (1935). Sugar detection by the ferricyanide electrode. J. Biol. Chem., 



Ill, 707. 



Shaner, V. C, and Sparks, M. R. (1945). Application of the polarograph to the analysis of photo- 

 graphic fixing baths. J . Soc. Motion Picture Engrs., 45, 20-32. 



Shapiro, H. (1939). Some functional correlatives of cellular metaboUsm. Cold Spring Harbor 

 Symposia Quant. Biol., 7, 408. 



Shibata, K., and Tamiya, H. (1930). Untersuchungen tiber die Bedeutung des Cytochroms in der 

 Physiologie der Zellatmung. Acta. Phyiochim., Tokyo, 5, 23. 



Shibuya, K., Saeki, H. and Ryv, K. (1936). The change of oxidation-reduction potentials of water- 

 logged soils. II. Lateritic soils and sandstone-shale soils. ./. Agr. Chem. Soc. Japan, 12, 

 1141-51. 



SmKATA and Tachi (1932). J. Chem. Soc, Japan, 53, 834. 



Simpson, G. K., and Traill, D. (1946). Polarographic Determination of Thyroxine and Diiodoty- 

 rosine. Biochem. J., 40, 116. 



SiZER, I. W. (1942). The activity of yeast invertase as a function of oxidation -reduction potential. 

 J. Gen. Physiol., 25, 399-409. 



and Tytell, A. A. (1941). The activity of crystalline urease as a function of oxidation-reduc- 

 tion potential. J. Biol. Chem.. 138, 631-42. 



Smadel, J. E., Jackson, E. B., Ley, H. L., and Lewthwaite, R. (1949). Proc. Soc. Exp. Biol. Med., 

 70, 191. 



Smith, E. L. (1948). Purification of anti-pernicious anaemic factors from liver. Nature, 161, 638. 



Smith, L. I., Kolthoff, I. M., Wawzonek, S., and Ruoff, P. M. (1941). Chemistry of vitamin E. 

 XXIX. Studies of the behaviour of compounds related to vitamin E at the dropping mercury 

 electrode. J. Am. Chem. Soc, 63, 1018-24. 



, Spillane, L. J. and Kolthoff, I. M. (1942). The chemistry of vitamin E. XXXV. The 



behaviour of tocopherols at the dropping mercury electrode. J. Am. Chem. Soc, 64, 447-51. 



, , (1942). Chemistry of vitamin E. XXXVI. Behaviour at the dropping mercury 



electrode of quinones related to vitamin E. J. Am. Chem. Soc, 64, 644-5. 



Smoler, I., see Heyrovsky and Smoler (1932). 



Spitta, D., and Weldert (1906). Indikatoren fiir die Beurteilung biologisch gereinigter Abwasser. 

 Mitt. Prufungsanst. Wasserversorg. Berlin, 6, 161. 



Standfast, A., see Wooldridge and Standfast (1933). 



Stannard, J. N. (1939). The mechanism involved in the transfer of oxygen in frog muscle. CoW 

 Spring Harbor Symposia Quant. Biol., 7, 394. 



Stansly, p. G., and Brownlee, G. (1949). Nomenclature of polymyxin antibiotics. Nature, 153, 611. 



•, Shepherd, R. G., and White, H. J. (1947). Bull. Johns Hopkins Hosp., 81, 43. 



Stake, F. J. (1935). Potentiometric study of hepatoflavin. /. Bio. Chem., 112, 223. 



and Baumann, C. A. (1939). Fumarate in biological oxidations. Cold Spring Harbor Sym- 

 posia Quant. Biol., 7, 227. 



Stephenson, M. (1928). On lactic dehydrogenase; a cell free enzyme preparation obtained from 

 bacteria. Biochem. Journ., 22, 605. 



(1949) Bacterial metabolism. London. 



and Stickland, L. H. (1931). Hydrogenase, a bacterial enzyme activating molecular hydrogen. 



I. II. Biochem. Journ., 25, 205, 215. 



, see also Quastel and Stephenson (1926). 



Stephenson, R. E., Schuster, C. E., and Spulnik, J. (1938). Oxidation-reduction potentials in 



orchard soils. J. Am. Soc Agron., 30, 91-6. 

 Stern, K.G. (1934). Potentiometric study of photo-flavin. Biochem. J., 28, 949. 



(1935). Oxidation reduction potentials of toxoflavin. Biochem. J., 29, oQO. 



(1939). Respiratorv catalysts in heart muscle. Cold Spring Harbor Symjiosia Quant. Biol., 



7, 312. 



and Greville, G. D. (1933). Uber Urochrom und die Teilnahme von Lyochromen an der 



Zellatmimg. Naturwiss., 21, 720. 



, see also Groville and Stern (1935). 



Stewart. C. P., see Morgan, Stewart and Hopkins (1922). 



Stickland, L. H. (1934). Studies in the metabolism of the strict anaerobes (genus Clostridium). L 

 Biochem. J., 28, 1746. 



(1935). Studies in the metabolism of the strict anaerobes (genus Clostridium), II. The reduction 



of proline by CI. sporogenes. Biochem. J.. 29, 288. 



(1949). The activation of phospiioglucomutase by metal ions. Biochem. J.. 44, IflO. 



, see also Green, Stickland and Tarr ( 1934). 



Stephenson and Stickland (1931). 



