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KMID : 0614619920240061423
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Korean Journal of Gastroenterology
1992 Volume.24 No. 6 p.1423 ~ p.1433
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Analysis of Human Pancreatic Juice Proteins by High Performance Liquid Chromatography Using Hydrophobic Interaction Column
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Abstract
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The human pancreas possesses an extraordinary capacity to synthesize and secrete a wide range of products, mainly the digestive enzymes. Knowledge of the secretory profiles of pancreatic exocrine enzyme is important for understanding of
physiological as
well as pathological processes in the pancreas. The present study was the first approach to resolve and characgeterizer enzymes in human pancreatic juice by HPLC using hydrophobic interaction column (HIC).
Pancreatic juice obtained from 14 human subjects was analyzed. Decreasing four-stage ammonium sulfate concentration in the gradient of mobile phase. it was possible to obtain an ideal chromatogram of human pancreatic juice protein. and total 18
peaks
were detected in the chromatogram. Analysis of enzymatic activity of each peak revealed 5 major enzymes, those were, trypsinogen, chymotrypsinogen. procarboxypeptidase A, procarboxypeptidase B. and amylase. The molecular weights of each enzyme
peak
was
identical to those reported previously by 2 dimensional electrophoresis.
There results suggest that the HPLC analysis of human pancreatic juice protein using HIC allows rapid and reproducible separation of the major enzyme proteins, and it may be useful in the diagnosis of human pancreatic diseases.
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KEYWORD
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