PHYSIOLOGY OF ADIPOSE TISSUE 621 



blood. The presence of diastase, 478 phosphatase, 479 lipase, 401 and dehydro- 

 genase 420 in adipose tissue has been demonstrated. In support of the 

 hypothesis that the diastase obtained from fatty tissues is an enzyme char- 

 acteristic of adipose tissue, Hausberger 464 demonstrated an increased con- 

 tent in denervated tissue; moreover, the activity of phosphatase is en- 

 hanced on recovery feeding. 378 These data are interpreted to mean that 

 the enzymes are formed in situ in adipose tissue. On the other hand, 

 Mirski 122 reported that blood diastase and "adipose diastase" are appar- 

 ently the same, since they act on glycogen in a similar manner to yield as 

 hydrolysis products non-fermentable low polysaccharides, rather than 

 glucose. However, Mirski was able to demonstrate a second pathway of 

 glycogen degradation in brown adipose tissue, which involves phosphoryla- 

 tion of glycogen and the subsequent formation of the Cori ester through the 

 mediation of phosphoglucomutase. The enzyme systems responsible for 

 this change were not found in white adipose tissue. 



The presence of dehydrogenases in adipose tissue is more firmly es- 

 tablished 419 ' 422 than is that of the diastase and phosphatase. Yosii 420 re- 

 ported that the dehydrogenase activity in adipose tissue is two to three 

 times that in liver and kidney, and thirty times that in muscle. For an 

 active enzyme preparation, phosphate and a boiled extract of adipose tissue 

 or yeast must be added to the dialyzed extracts of adipose tissue. 421 The 

 co-factor in the boiled extract has been shown to be adenosine-5-phosphoric 

 acid. 421 ' 480 In contradistinction to the properties of other dehydrogen- 

 ases, 481 those from adipose tissue appear to be concerned only with desatura- 

 tion and not with the total breakdown of the fatty acids. 480 



The presence of lipolytic enzymes (lipases) in the adipose tissue has been 

 noted by a number of investigators. Quagliariello and Scoz 482 reported 

 that the hydrolysis of both triolein and tributyrin was catalyzed by an ex- 

 tract of the adipose tissue of the dog. The activity of adipose lipase was 

 only 1% that of the same weight of dried pancreas, and approximately the 

 same as that of dried stomach, but it was twenty-five times that of the 

 same weight of dried liver. On the basis of histologic tests, Gomori 483 ' 484 



478 F. X. Hausberger and N. Neuenschwander-Lemmer, Arch, exptl. Pathol. Pharmakol. 

 (Naunyn-Sch?niedeberg's), 192, 530-535 (1939). 



479 F. X. Hausberger and N. Neuenschwander-Lemmer, Arch, exptl. Pathol. Pharma- 

 kol. (Naunyn-Schmiealeberg's), 193, 110-116 (1939). 



4S0 O. S. A. K. Lang and H. Mayer, Z. physiol. Chem., 261, 249-252 (1939). 



481 L. F. Leloir and S. M. Munoz, Biochem. J., 82, 299-307 (1938). 



482 G. Quagliariello and G. Scoz, Arch. set. biol. (Italy), 17, 513-529 (1932). 



483 G. Gomori, Arch. Pathol., 41, 121-129 (1946). 



484 G. Gomori, Proc. Soc. Exptl. Biol. Med., 58, 362-364 (1945). 



