Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 37: 361-368, 1991;
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lott, J. A.
Right arrow Articles by Lu, C. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lott, J. A.
Right arrow Articles by Lu, C. J.

Clinical Chemistry, Vol 37, 361-368, Copyright © 1991 by American Association for Clinical Chemistry

Lipase isoforms and amylase isoenzymes: assays and application in the diagnosis of acute pancreatitis

JA Lott and CJ Lu
Department of Pathology, Ohio State University, Columbus.

Pancreatic juice and serum from patients with acute pancreatitis contain three enzymes that have lipolytic activity: L1 and L2, which are pancreatic isoenzymes or isoforms of lipase (EC 3.1.1.3), and L3, which is probably pancreatic carboxyl ester lipase, also known as cholesterol esterase (EC 3.1.1.13). These enzymes are readily separated electrophoretically on agarose and can be developed with an overlay of Kodak Ektachem lipase slide material. The latter acts as a dry-reagent developing substrate, with the enzymes producing blue bands in the slide material. We found L1 in about one-half of normal persons, L2 in none, and L3 in all. We assayed for amylase (EC 3.2.1.1), amylase isoenzymes, lipase, and lipase isoforms in the sera of 100 patients with suspected acute pancreatitis. L2 lipase has the greatest diagnostic efficiency for the diagnosis of pancreatitis, compared with total amylase, P3 amylase, and total lipase. Lipase and L2 could replace amylase, an inefficient test, for the diagnosis of patients with suspected acute pancreatitis. In patients receiving organ transplants, a serum amylase value of greater than 300 U/L or a lipase of greater than 1000 U/L discriminated well between patients with and without complications and (or) acute rejection.


The following articles in journals at HighWire Press have cited this article:


Home page
 Clin. Chem.Home page
Y. E. Taes, H. Louagie, J.-P. Yvergneaux, M. L. De Buyzere, H. De Puydt, J. R. Delanghe, and J. A. Lott
Prolonged Hyperlipasemia Attributable to a Novel Type of Macrolipase
Clin. Chem., December 1, 2000; 46(12): 2008 - 2013.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Chem.Home page
G. Diani, G. Poma, F. Novazzi, S. Zanirato, C. Porta, M. Moroni, G. V. M. d'Eril, and R. Moratti
Increased Serum Lipase with Associated Normoamylasemia in Cancer Patients
Clin. Chem., May 1, 1998; 44(5): 1043 - 1045.
[Full Text] [PDF]

Home page
 Clin. Chem.Home page
M. Munoz-Perez, D. Sarrion-Pelous, J. Jimenez-Jimenez, P. Martinez-Montiel, and M. Gallego-Valdes
Chronic Increased Serum Lipase in a Patient with Suspected Pancreatic Adenocarcinoma
Clin. Chem., January 1, 1997; 43(1): 191 - 193.
[Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1991 by the American Association for Clinical Chemistry.