18 II. DIGESTION AND ABSORPTION OF FATS 



acid chain is of more importance in affecting the activity of esterase than 

 is the type of alcohol to which it is attached. 106 Alper and collaborators 106 

 reported that the action of serum esterase is determined by chain length 

 and by type of glyceride as follows : 



Triacetin > Diacetin > Monoacetin 

 Tripropionin > Monopropionin 

 Tributyrin > Monobutyrin 

 Monoolein > Triolein 

 Tripropionin > Tributyrin > Triacetin 



Alper et al. m state that serum esterase resembles liver esterases more than 

 it does pancreatic lipase. 



The optical activity of the substrate esters, likewise, is a factor by which 

 the specificity of esterases can be demonstrated. Beef liver esterase and 

 that from carp liver show a preferential splitting of L-tartaric acid esters 

 over those of the D-form. 85 On the other hand, esterase from pig liver 

 hydrolyzes preferentially the esters of d-mandelic acid in a mixture of d- 

 and L-esters; pancreatic esterase attacks mainly the esters of L-mandelic 

 acid. 107 



Serum lipase was sfkown to decrease in rats on the first to third day after 

 the administration of alloxan. 108 It is not affected by thyroidectomy in the 

 rabbit. 109 A decreased level of tributyrinase, as compared with the normal, 

 was reported in hypertensive and arteriosclerotic human males, but the 

 level of this enzyme was not altered in females suffering from these condi- 

 tions. 110 In the nutritional disease of children known as "kwashiorkor," 

 subnormal plasma esterase and plasma lipase values were reported by 

 Srinivasan and Patwardhan. 111 Komarov et al. 112 were unable to note any 

 correlation between tributyrinase and lipolytic activity in different speci- 

 mens of pancreatic secretion and of blood sera. 



e. Preparation of Esterases. Liver esterase has been prepared by a 

 variety of procedures. The original preparation of Dakin 113 was a crude 

 press juice of pig liver ground with kieselguhr. Peirce 114 carried out a 



105 A. K. Balls, M. B. Matlack, and I. W. Tucker, J. Biol. Chem., 122, 125-137 (1937- 

 1938). 



106 C. Alper, P. P. Polakoff, Jr., and E. Alexander, Federation Proc, 12, 167-168 (1953). 



107 R. Willstatter and F. Memmen, Z. physiol. Chem., 138, 216-253 (1924). 



108 J. Tuba and R. Hoare, Science, 110, 168 (1949). 



109 G. Weber and K. Drechsler, Am. J. Physiol., 162, 289-292 (1950). 



110 A. Bernhard and A. Rothenberg, Proc. Soc. Exptl. Biol. Med., 78, 533-535 (1951). 



111 P. R. Srinivasan and V. N. Patwardhan, Lancet, 263, 864-866 (1952). 



112 S. Komarov, H. Shay, and C. Zislin, Federation Proc, 12, 80 (1953). 



113 H. D. Dakin, J. Physiol, 32, 199-206 (1904). 



114 G. Peirce, J. Biol. Chem., 16, 1-3 (1913). 



