9. COMPARATIVE BIOCHEMISTRY OF GLYCOLYSIS
43i
istration of subcurative doses of stibophen to the host results in an accumulation of the substrate (fructose-6-phosphate) and a decrease of
the product (fructose-l,6-diphosphate) of the phosphofructokinase reaction within the parasite (181).
While the specificity of homologous glycolytic enzymes for various
species and tissues has been demonstrated, there is no evidence that
glycolytic enzymes of muscle and of tumors of the same animal differ
from each other. Kubowitz and Ott (237) have found that immunologically, as well as kinetically, the lactic dehydrogenases of rat muscle
and of Jensen rat sarcoma are indistinguishable from each other. Similar
results have been obtained with aldolase of rabbit muscle and of rabbit
Brown-Pearce tumor cells (238). .
From the foregoing, it is evident that differences exist in the nature
of glycolytic enzymes which catalyze the same reactions in different
species and tissues. Such differences may occur at various levels. In some
cases, homologous glycolytic enzymes may be distinguished only by the
use of specific antibodies. In other instances, such enzymes differ from
each other not only immunologically but also in their affinities for their
substrates, in the effect of the hydrogen ion concentration on their activities, and in their cofactor requirements. In other cases, differences
in substrate specificities as well as in kinetics are encountered. Finally,
certain compounds interfere with the functional integrity of a glycolytic
enzyme of one species, but not with that of another. Such differences
are pertinent to an understanding of the mechanism of action and to
the rational development of chemotherapeutic agents; it remains to be
determined whether and in what manner such variations can be related
to biochemical evolution and adaptation.
References
1. H. A. Krebs and H. L. Kornberg, Ergeh. Physiol. 49, 212-298 (1957).
2. G. Gomori, /. Biol. Chem. 148, 139-149 (1943).
3. H. G. Hers, Biochim. et Biophys. Acta 8, 416-423 (1952).
4. L. C. Mokrasch and R. W. McGilvery, /. Biol. Chem. 221, 909-917 (1956).
5. G. T. Cori, C. F. Cori, and G. Schmidt, /. Biol. Chem. 129, 629-639 (1939).
6. M. A. Swanson, /. Biol. Chem. 184, 647-659 (1950).
7. R. Levine, M. S. Goldstein, B. Huddlestun, and S. P. Klein, Am. J. Physiol.
163, 70-76 (1950).
8. M. S. Goldstein, V. Mullick, B. Huddlestun, and R. Levine, Arn. J. Physiol.
173, 207-216 (1953).
9. C. R. Park, R. L. Post, C. F. Kaiman, J. H. Wright, Jr., L. H. Johnson, and
H. E. Morgan, Ciha Fdn. Colloquia Endocrin. 9, 240-260 (1956).
10. C. R. Park, J. Bornstein, and R. L. Post, Am. J. Physiol. 182, 12-16 (1955).
11. C. R. Park and L. H. Johnson, Am. J. Physiol. 182, 17-23 (1955).
12. C. R. Park, L. H. Johnson, and J. H. Wright, Jr., Federation Proc. 15, 324
(1956).
43i
istration of subcurative doses of stibophen to the host results in an accumulation of the substrate (fructose-6-phosphate) and a decrease of
the product (fructose-l,6-diphosphate) of the phosphofructokinase reaction within the parasite (181).
While the specificity of homologous glycolytic enzymes for various
species and tissues has been demonstrated, there is no evidence that
glycolytic enzymes of muscle and of tumors of the same animal differ
from each other. Kubowitz and Ott (237) have found that immunologically, as well as kinetically, the lactic dehydrogenases of rat muscle
and of Jensen rat sarcoma are indistinguishable from each other. Similar
results have been obtained with aldolase of rabbit muscle and of rabbit
Brown-Pearce tumor cells (238). .
From the foregoing, it is evident that differences exist in the nature
of glycolytic enzymes which catalyze the same reactions in different
species and tissues. Such differences may occur at various levels. In some
cases, homologous glycolytic enzymes may be distinguished only by the
use of specific antibodies. In other instances, such enzymes differ from
each other not only immunologically but also in their affinities for their
substrates, in the effect of the hydrogen ion concentration on their activities, and in their cofactor requirements. In other cases, differences
in substrate specificities as well as in kinetics are encountered. Finally,
certain compounds interfere with the functional integrity of a glycolytic
enzyme of one species, but not with that of another. Such differences
are pertinent to an understanding of the mechanism of action and to
the rational development of chemotherapeutic agents; it remains to be
determined whether and in what manner such variations can be related
to biochemical evolution and adaptation.
References
1. H. A. Krebs and H. L. Kornberg, Ergeh. Physiol. 49, 212-298 (1957).
2. G. Gomori, /. Biol. Chem. 148, 139-149 (1943).
3. H. G. Hers, Biochim. et Biophys. Acta 8, 416-423 (1952).
4. L. C. Mokrasch and R. W. McGilvery, /. Biol. Chem. 221, 909-917 (1956).
5. G. T. Cori, C. F. Cori, and G. Schmidt, /. Biol. Chem. 129, 629-639 (1939).
6. M. A. Swanson, /. Biol. Chem. 184, 647-659 (1950).
7. R. Levine, M. S. Goldstein, B. Huddlestun, and S. P. Klein, Am. J. Physiol.
163, 70-76 (1950).
8. M. S. Goldstein, V. Mullick, B. Huddlestun, and R. Levine, Arn. J. Physiol.
173, 207-216 (1953).
9. C. R. Park, R. L. Post, C. F. Kaiman, J. H. Wright, Jr., L. H. Johnson, and
H. E. Morgan, Ciha Fdn. Colloquia Endocrin. 9, 240-260 (1956).
10. C. R. Park, J. Bornstein, and R. L. Post, Am. J. Physiol. 182, 12-16 (1955).
11. C. R. Park and L. H. Johnson, Am. J. Physiol. 182, 17-23 (1955).
12. C. R. Park, L. H. Johnson, and J. H. Wright, Jr., Federation Proc. 15, 324
(1956).