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THE HISTOCHEMICAL DEMONSTRATION OF PANCREATIC-LIKE LIPASE AND COMPARISON WITH THE DISTRIBUTION OF ESTERASE

MUNEAKI ABE 1, STANLEY P. KRAMER 1, and ARNOLD M. SELIGMAN 1

1 From the Departments of Surgery, Sinai Hospital of Baltimore, and The Johns Hopkins University School of Medicine, Baltimore, Md.

A new histochemical method for lipase was developed using naphthol-AS nonanoate as a substrate and sodium taurocholate as an activator. In a comparison with esterase, pancreatic-like lipase activity was studied in various tissues. As a result, it was disclosed that the pancreatic acinar cells show the highest activation with sodium taurocholate, and lipase activity is located in the region immediately surrounding the zymogen granules and not within the granules themselves.

Maximum activity of esterase and lipase differed among various tissues of the rat. Esterase activity is most intense in liver and kidney followed by pancreas. Pancreatic-like lipase activity is most striking in pancreas, less so in the liver and in the kidney the activity is rather weak. Because of the exceptional esterase activity of macrophages, mast cells and pericytes of the cerebral capillaries, pancreatic-like lipase activity should be ascribed to them with caution and only in terms of the difference between reaction without and with sodium taurocholate.

Submitted on September 23, 1963


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