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PMID: 6607205 Published · ppublish English Journal Article

Alpha 1-proteinase inhibitor in pure human pancreatic juice. Characterization of a complexed form in patients with chronic calcifying pancreatitis and its significance.

Hoppe-Seyler's Zeitschrift fur physiologische Chemie ·Vol. 364 ·No. 11 ·1983-11-00 ·Pages 1597-601

Miszczuk-Jamska B, Guy O, Figarella C

Abstract

Two forms of alpha 1-proteinase inhibitor (alpha 1-PI) were characterized in the pancreatic juice of patients with chronic pancreatitis, one free form and one form complexed with a proteinase. This complex is probably present in minute amounts in normal pancreatic juice which contains mainly free alpha 1-PI. The proteinase bound to alpha 1-PI has been identified as chymotrypsin A and the inhibitory activity of the free form of alpha 1-PI has been demonstrated. These data underline the rapid conversion of human proteolytic zymogens into active enzymes and demonstrate the increase of this activation phenomenon in the juice of patients with chronic pancreatitis.

MeSH Terms
Blood Proteins/isolation & purification Chronic Disease Chymotrypsin/antagonists & inhibitors Humans Immunoelectrophoresis, Two-Dimensional Pancreatic Juice/analysis,enzymology Pancreatitis/physiopathology alpha 1-Antitrypsin
Chemicals
Blood Proteins alpha 1-Antitrypsin Chymotrypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Miszczuk-Jamska B
Guy O
Figarella C
Article Info
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Abbr.
Hoppe Seylers Z Physiol Chem
ISSN
0018-4888
Published
1983-11-00
Pages
1597-601
Language
English
Region
Germany
NLM ID
2985060R
Subset
IM
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