3. MECHANISMS FOR FATTY ACID OXIDATION
103
what is the true role of lipoxidase and of lipase? There is a common
denominator in the comparative biochemistry of fatty acid oxidation;
namely ^-oxidation. Superimposed on this are the variants that have
developed in different tissues in response to their own needs. In some
cases the life of the cell depends on the development and amplification
of these variants but in other cases these play only a minor role. This
chapter has attempted to point out these variants and indicate their
relative importance.*
References
1. G. S. Parks and H. M. Huffman, "The Free Energies of Some Organic Compounds," p. 136. Chemical Catalog, New York, 1932.
2. H. Beinert, D. E. Green, P. Hele, H. Hift, R. W. Von Korff, and C. V. Ramakrishnan, /. Biol. Chem. 203, 35-45 (1953); W. P. Jencks and F. Lipmann,
ibid. 225, 207-223 (1957).
3. A. Millerd and J. Bonner, Arch. Biochem. Biophys. 49, 343-355 (1954).
4. P. K. Stumpf and G. A. Barber, /. Biol. Chem. 227, 407-417 (1957).
5. P. Berg, /. Biol. Chem. 222, 991-1013 (1956).
6. M. A. Eisenberg, Biochim. et Biophys. Ada 16, 58-65 (1955).
7. A. Kornberg and W. E. Pricer, Jr., /. Biol. Chem. 204, 329-343 (1953).
8. A. W. D. Avison, /. Chem. Soc. pp. 732-738 (1955).
9. W. P. Jencks, Biochim. et Biophys. Ada 24, 227-228 (1957).
10. E. R. Stadtman, /. Biol. Chem. 203, 501-512 (1953).
11. J. R. Stern, M. J. Coon, A. del Campillo, and M. C. Schneider, /. Biol. Chem.
221, 15-31 (1956).
12. E. R. Stadtman, /. Biol. Chem. 196, 527-534, 535-546 (1952).
13. T. A. M. Rose, M. Grunberg-Manago, S. R. Korey, and S. Ochoa, /. Biol. Chem.
211, 737-756 (1954).
14. F. Lipmann, /. Biol Chem. 155, 55-70 (1944).
15. G. Kalnitsky and C. H. Werkman, Arch. Biochem. 2, 113-124 (1943).
16. B. L. Horecker, E. C. Heath, J. Hurwitz, and A. Ginsburg, Federation Proc.
16, 198 (1957).
17. H. J. Koepsell and M. J. Johnson, /. Biol. Chem. 145, 379-386 (1942).
18. J. Gergely, in "Methods in Enzymology" (S. Colowick and N. O. Kaplan, eds.),
Vol. I, pp. 602-607. Academic Press, New York, 1955.
19. J. R. Stern, M. J. Coon, and A. del Campillo, Nature 171, 28-30 (1953).
20. J. R. Stern, A. del Campillo, and A. L. Lehninger, J. Am. Chem. Soc. 77,
1073-1074 (1955).
21. W. P. McCann, /. Biol. Chem. 226, 15-22 (1957).
22. W. Seubert, G. Greull, and F. Lynen, Angew. Chem. 69, 359-361 (1957).
23. H. S. Moyed and F. Lipmann, /. Bacteriol. 73, 117-121 (1957).
24. D. E. Green, S. Mii, H. R. Mahler, and R. M. Bock, /. Biol. Chem. 206, 1-12
(1954).
25. F. L. Crane, S. Mii, J. G. Hauge, D. E. Green, and H. Beinert, J. Biol. Chem.
218, 701-710 (1956).
* Note added in proof: Recent developments in this field have been discussed by
Stumpf (80).
103
what is the true role of lipoxidase and of lipase? There is a common
denominator in the comparative biochemistry of fatty acid oxidation;
namely ^-oxidation. Superimposed on this are the variants that have
developed in different tissues in response to their own needs. In some
cases the life of the cell depends on the development and amplification
of these variants but in other cases these play only a minor role. This
chapter has attempted to point out these variants and indicate their
relative importance.*
References
1. G. S. Parks and H. M. Huffman, "The Free Energies of Some Organic Compounds," p. 136. Chemical Catalog, New York, 1932.
2. H. Beinert, D. E. Green, P. Hele, H. Hift, R. W. Von Korff, and C. V. Ramakrishnan, /. Biol. Chem. 203, 35-45 (1953); W. P. Jencks and F. Lipmann,
ibid. 225, 207-223 (1957).
3. A. Millerd and J. Bonner, Arch. Biochem. Biophys. 49, 343-355 (1954).
4. P. K. Stumpf and G. A. Barber, /. Biol. Chem. 227, 407-417 (1957).
5. P. Berg, /. Biol. Chem. 222, 991-1013 (1956).
6. M. A. Eisenberg, Biochim. et Biophys. Ada 16, 58-65 (1955).
7. A. Kornberg and W. E. Pricer, Jr., /. Biol. Chem. 204, 329-343 (1953).
8. A. W. D. Avison, /. Chem. Soc. pp. 732-738 (1955).
9. W. P. Jencks, Biochim. et Biophys. Ada 24, 227-228 (1957).
10. E. R. Stadtman, /. Biol. Chem. 203, 501-512 (1953).
11. J. R. Stern, M. J. Coon, A. del Campillo, and M. C. Schneider, /. Biol. Chem.
221, 15-31 (1956).
12. E. R. Stadtman, /. Biol. Chem. 196, 527-534, 535-546 (1952).
13. T. A. M. Rose, M. Grunberg-Manago, S. R. Korey, and S. Ochoa, /. Biol. Chem.
211, 737-756 (1954).
14. F. Lipmann, /. Biol Chem. 155, 55-70 (1944).
15. G. Kalnitsky and C. H. Werkman, Arch. Biochem. 2, 113-124 (1943).
16. B. L. Horecker, E. C. Heath, J. Hurwitz, and A. Ginsburg, Federation Proc.
16, 198 (1957).
17. H. J. Koepsell and M. J. Johnson, /. Biol. Chem. 145, 379-386 (1942).
18. J. Gergely, in "Methods in Enzymology" (S. Colowick and N. O. Kaplan, eds.),
Vol. I, pp. 602-607. Academic Press, New York, 1955.
19. J. R. Stern, M. J. Coon, and A. del Campillo, Nature 171, 28-30 (1953).
20. J. R. Stern, A. del Campillo, and A. L. Lehninger, J. Am. Chem. Soc. 77,
1073-1074 (1955).
21. W. P. McCann, /. Biol. Chem. 226, 15-22 (1957).
22. W. Seubert, G. Greull, and F. Lynen, Angew. Chem. 69, 359-361 (1957).
23. H. S. Moyed and F. Lipmann, /. Bacteriol. 73, 117-121 (1957).
24. D. E. Green, S. Mii, H. R. Mahler, and R. M. Bock, /. Biol. Chem. 206, 1-12
(1954).
25. F. L. Crane, S. Mii, J. G. Hauge, D. E. Green, and H. Beinert, J. Biol. Chem.
218, 701-710 (1956).
* Note added in proof: Recent developments in this field have been discussed by
Stumpf (80).