Histochemistry of Hepatic Phosphatases at a Physiologic pH: With Special Reference to the Demonstration of Bile Canaliculi

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Abstract
A modified lead phosphate technic for the demonstration of nonspecific phosphatase, 5-nucleotidase and adenosine tri-phosphatase at pH 7.2 was applied to fresh and cold formalin-fixed frozen sections from the liver of dog, rat, mouse, rabbit, guinea pig, and man. In addition, sections were stained for histochemically demonstrable glucose-6-phosphatase. The latter enzyme can be demonstrated in the liver of all these species, even in human autopsy material under favorable conditions. Nonspecific phosphatase gives a considerably stronger reaction in hepatic cells at pH 7.2 than at pH 9, indicating that nonspecific phosphatase may be of considerable importance in hepatic metabolism at a physiologic pH. The sinusoids are particularly well outlined in sections stained for 5-nucleotidase activity. The adenosine triphosphatase technic applied to formalin-fixed sections permits an excellent and uniform demonstration of the biliary canaliculi in all species examined. The regularity with which these structures are demonstrable makes the adenosine triphosphatase technic a useful tool for the study of the intrahepatic biliary system under normal and abnormal conditions.