472 C. F. Strittmatter 



or TPNH and molecular oxygen might be combined to produce the grouping 

 required for biological hydroxylation reactions. However, there is at present 

 no direct evidence for participation of microsomal cytochrome in hydroxy- 

 lation or other synthetic processes. 



Clearly, the question of the biological functions of microsomal cytochrome 

 and other apparently related cytochrome ^5-like substances is still unanswered, 

 but the lively current interest in this problem gives hope that further insight 

 into the biological significance of these compounds may be obtained in the 

 near future. 



REFERENCES 

 Appleby, C. A. & Morton, R. K. (1954). Nature, Loncl. 173, 749. 

 Bailie, M. & Morton, R. K. (1955). Nature, Loud. 176, 111. 

 Bailie, M. & Morton, R. K. (1958). Biochem. J. 69, 35. 

 BucHER, N. L. R. & McGarrahan, K. (1953). /. biol. Chem. Ill, 1. 

 Chaix, p. & Heyman-Blachet, T. (1957). Biochim. biophys. Acta 26, 214. 

 Chance, B. & Williams, C. R. (1954). /. biol. Chem. 209, 945. 

 Chance, B. & Williams, G. R. (1955). /. biol. Chem. Ill, 395. 

 Ephrussi, B. & Slonimski, p. P. (1950). Biochim. biophys. Acta 6, 256. 

 FujiTA, A. & KoDAMA, T. (1934). Biochem. Z. 113, 186. 

 Garfinkel, D. (1957). Arch. Biochem. Biophys. 71, 111. 

 Hayes, J. E. Jr. & Velick, S. F. (1954). /. biol. Chem. 207, 225. 

 Hill, R. & Scarisbrick, R. (1951). New Phytol. 50, 98. 



HoGEBOOM, G. H., Claude, A., Hotchkiss, R. D. (1946). /. biol. Chem. 165, 615. 

 HoGEBOOM, G. H. (1949). /. biol. Chem. Ill, 847. 



Hulsman, W. C, Elliott, W. B. & Rudney, H. (1958). Biochim. biophys. Acta 11, 663. 

 HuszAK, I. (1942). Biochem. Z. 312, 330. 

 Keilin, D. (1925). Proc. roy. Soc. 5 98, 312. 

 Keilin, D. (1933). Ergebn. Enzymforsch. 2, 239. 

 Keilin, D. (1934). Nature, Lond. 133, 290. 

 Keilin, D. & Hartree, E. F. (1940). Proc. roy. Soc. B 129, 277. 

 Keilin, D. & Hartree, E. F. (1947). Biochem. J. 41, 503. 

 Keilin, D. & Hartree, E. F. (1949). Nature, Lond. 164, 254. 



Kersten, H., Leonhauser, S. & Staudinger, H. (1958). Biochim. biophys. Acta 29, 350. 

 Kersten, H., Kersten, W. & Staudinger, H. (1958). Biochim. biophys. Acta 11, 598. 

 Klingenberg, M. (1958). Arch. Biochem. Biophys. 75, 376. 

 Krisch, K. & Staudinger, H. (1958). Biochem. Z. 331, 37. 

 Kun, E. (1951). Proc. Soc. exp. Biol. N.Y. 11, 441. 

 Littlefield, J. W., Keller, E. B., Gross, J. «& Zamecnik, P. C. (1955). J. biol. Chem. Ill, 



11. 

 MacMunn, C. a. (1884). /. Physiol. 5, Proc. xxiv. 

 MacMunn, C. a. (1886). Phil. Trans. Ill, 267. 

 Mahler, H. R., Raw, I., Molinari, R. & doAmaral, D. F. (1958). /. biol. Chem. 233, 



230. 

 Martin, E. M. & Morton, R. K. (1955). Nature, Lond. 176, 113. 

 Martin, E. M. & Morton, R. K. (1957). Biochem. J. 65, 404. 

 Mason, H. S. (1957). Advanc. Enzymol. 19, 79. 



Palade, G. E. & SiEKEVTTZ, P. (1956). J. Biochem. Biophys. Cytol. 2, 671, 

 Pappenheimer, a. M. & Williams, C. M. (1954). /. biol. Chem. 209, 915. 

 Raw, I., Molinari, R., doAmaral, D. F. & Mahler, H. R. (1958). /. biol. Chem. 233, 225. 

 Raw, I. & Mahler, H. R. (1959). /. biol. Chem. 134, 1867. 

 Ryan, K. & Engel, L. L. (1957). /. biol. Chem. 225, 103. 

 Sanborn, R. C. & Williams, C. M. (1950). /. gen. Physiol. 33, 579. 

 Schneider, W. C. & Hogeboom, G. H. (1956). Annu. Rev. Biochem. 25, 201. 



