178 III. OXIDATION AND METABOLISM 



gjg_32, 33,581-689 Qj^ ^Jjq other haiid, liver slices from rats are able to destroy 

 ketone bodies under anaerobic and aerobic conditions.^^'*'^^'' Malonic 

 acid acts as an agent inhibiting this reaction. 



The rate of spontaneous ketogenesis is accelerated in liver slices obtained 

 from fasted rats, and is depressed in slices from well-fed animals when the 

 substrate contains no ketone bodies or when butyrate is present.^^^"^^* 

 Moreover, Cohen and Stark^^^ reported that, when an acetoacetate sub- 

 strate was employed, the rate of ketone body disappearance was greater 

 in preparations of liver from well-fed rats, rabbits, and guinea pigs than in 

 slices from the livers of fasted animals of the same species. Quastel and 

 Wheatley^^* reported that glycogen (but not D-glucose) reduced the 

 Q02 and ketone body production of liver slices from fasted rats which were 

 immersed in a substrate containing butyrate, crotonate, or caproate. 

 In one series of tests, it was found that the addition of propionate to a 

 substrate containing butyrate caused a marked depression in acetoacetate 

 utilization, although these workers were unable to duplicate the results a 

 year later.^^^ The positive results were attributed to a substrate competi- 

 tion between propionate and butyrate,^^^ although the authors suggest 

 that the results might likewise be attributed to ketolysis. However, on the 

 basis of a reduced Q02, they concluded that antiketogenesis rather than 

 ketolysis best explained the lowered ketone body formation in liver slices 

 with a glycogen substrate. ^^"^ Cohen and Stark^^^ attributed similar re- 

 sults to ketolysis. 



The experiments of Bobbitt and Deuel^^^ likewise indicate that ketolysis 

 is the theory which best explains the action of carbohydrate on ketone 

 body disappearance. It was demonstrated in these tests not only that the 



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682 G. Embden and H. Engel, Beitr. chem. Physiol. Pathol, 11, 232-326 (1908); G. 

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683 M. Almagia and G. Embden, Beitr. cheyn. Physiol Pathol, 6, 59-62 (1905). 



68^1. Snapper and A. Griinbaum, Biochem. Z., ISl, 410-417, 418-424 (1927); 185, 

 223-228 (1927). 



686 1. Snapper, A. Griinbaum, and J. Neuberg, Biochem. Z., 167, 100-106 (1926). 



686 H. E. Himwich, W. Goldfarb, and A. Weller, /. Biol Chem., 93, 337-342 (1931). 



687 W. Goldfarb and H. E. Himwich, J. Biol. Chem., 101, 441-448 (1933). 



688 H. C. Harrison and C. N. H. Long, /. Biol Chem., 133, 209-218 (1940). 



689 1. A. Mirsky, Am. J. Physiol, 115, 424-428 (1936). 



690 1. E. Stark and P. P. Cohen, /. Biol Chem., 123, cxv (1938). 



691 B. G. Bobbitt and H. J. Deuel, Jr., /. Biol Chem., US, 1-9 (1942). 



692 S. Weinhouse, R. H. MiUington, and B. Friedman, /. Biol Chem., 181, 489-498 

 (1949). 



693 p. p. Cohen and I. P. Stark, /. Biol Chem., 126, 97-107 (1938). 



694 J. H. Quastel and A. H. M. Wheatley, Biochem. J., 27, 1753-1762 (1933). 

 696 J. H. Quastel and A. H. M. Wheatley, Biochem. J., 28, 1014-1027 (1934). 



