J.Jpn. Surg. Soc.. 84(9): 744-748, 1983

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Report on the annual meeting

PURIFICATION AND DEVELOPMENT OF IMMUNOASSAY FOR PANCREATIC ENZYMES AND TRYPSIN INHIBITOR, AND THEIR APPLICATION TO ELUCIDATION OF PATHOGENESIS OF VARIOUS PANCREATIC AND PANCREATIC ENZYME-PRODUCING DISEASES

Pancreatic amylase, elastase 1, elastase 2, cationic trypsin, chymotrypsin, ribonuclease (RNase), phospholipase A₂, γ-glutamyl transpeptidase (γ-GTP) and pancreatic secretory trypsin inhibitor (PSTI) were purified and characterized from human pancreatic juice and pancreatic tissue. During the purification of these enzymes, two enzymes previously not reported were found. A pancreatic deamidase and a renal endopeptidase were purified and characterized.
Specific and reliable radioimmunoassays (RIAs) were developed for all pancreatic enzymes and inhibitor. The purpose of immonoassay for pancreatic enzymes and inhibitor was discussed, and clinical application for the diagnosis of pancreatic diseases was demonstrated.
Messenger RNA (mRNA) of amylase was isolated from human pancreas and parotis, and used to prepare a complementary DNA (cDNA). The nucleotide sequence and the predicted amino acid sequence of these clones were now being determined. The application of the present investigation to elucidation of pathogenesis of pancreatic enzyme-producing diseases was discussed.

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