期刊名称：Journal of Clinical Biochemistry and Nutrition
印刷版ISSN：0912-0009
电子版ISSN：1880-5086
出版年度：1994
卷号：16
期号：1
页码：67-75
DOI：10.3164/jcbn.16.67
出版社：The Society for Free Radical Research Japan
摘要：Anti-human pancreatic elastase 1 autoantibodies occurring in sera of patients with pancreatic diseases specifically bound elastase 1 but showed little binding with proelastase 1. Binding of proelastase 1 to the autoantibodies was effectively elevated by tryptic digestion of the proelastase 1 for activation, suggesting that the autoantibodies recognized some conformational change from proelastase 1 to elastase 1. Gel filtration analysis of the 125I-labeled elastase 1 and proelastase 1 added to sera revealed that both elastase 1 and proelastase 1 existed as conjugates with α1-antitrypsin or α2-macroglobulin in autoantibody-negative sera; but in autoantibody-positive sera, more than 80% of elastase 1 was assumed to form an immune complex with the autoantibodies, while proelastase 1 did not seem to form an immune complex, but existed as conjugates with the serum protease inhibitors as was the case of autoantibody-negative serum. Therefore, conversion of proelastase 1 into the active form does not seem to occur in serum. These results indicate that anti-elastase 1 autoantibodies are produced as a consequence of the leakage of unusually large amounts of elastase 1 into the circulation after an attack of pancreatitis.
关键词：pancreatic elastase 1;pancreatic proelastase 1;autoantibody;binding specificity;conjugation form
