Differentiation of Human Phospholipase A 2 Isoenzymes in Serum and Other Body Fluids with Use of Monoclonal Antibodies

Differentiation of Human Phospholipase A 2 Isoenzymes in Serum and Other Body Fluids with Use of... Introduction Serum phospholipase A2 (EC 3.1.1.4) has long been assumed to originate exclusively from the pancreas (for review see 1. c. (1)). More recently, this assumption has been challenged by our group (1 --4) and other authors (5--7). In 1988, Eskolq et al. (6) demonstrated the existence of two different forms of phospholipase A2 in human serum using polyclonal antibodies against the pancreatic isoenzyme. Their study design, however, did not unequivocally prove that one of these "isoenzymes" * This work is part of the doctoral thesis of C. Dosser (Med. Fakultät of the Ludwig-Maximilians-Universität München, in preparation). Eur. J. Clin. Chem. Clin. Biochem. / Vol. 31,1993 / No. 4 was pancreatic phospholipase A2; since phospholipases A2 possess a highly conserved protein structure (8, 9), polyclonal antibodies against the pancreatic enzyme might cross-react with structurally related" isoenzymes. Immuno-reactive proteins have been found in serum of patients with non-pancreatic malignant tumours (10) as well as in rat spleen (11). On the other hand, most phospholipases A2 have a marked tendency to bind to proteins and surfaces in an unspecific manner (3, 12, 13), so that antibodyindependent binding artifacts may occur. The present article describes a practicable combination of activity measurements http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Clinical Chemistry and Laboratory Medicine de Gruyter

Differentiation of Human Phospholipase A 2 Isoenzymes in Serum and Other Body Fluids with Use of Monoclonal Antibodies

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Publisher
de Gruyter
Copyright
Copyright © 2009 Walter de Gruyter
ISSN
1434-6621
eISSN
1437-4331
DOI
10.1515/cclm.1993.31.4.211
Publisher site
See Article on Publisher Site

Abstract

Introduction Serum phospholipase A2 (EC 3.1.1.4) has long been assumed to originate exclusively from the pancreas (for review see 1. c. (1)). More recently, this assumption has been challenged by our group (1 --4) and other authors (5--7). In 1988, Eskolq et al. (6) demonstrated the existence of two different forms of phospholipase A2 in human serum using polyclonal antibodies against the pancreatic isoenzyme. Their study design, however, did not unequivocally prove that one of these "isoenzymes" * This work is part of the doctoral thesis of C. Dosser (Med. Fakultät of the Ludwig-Maximilians-Universität München, in preparation). Eur. J. Clin. Chem. Clin. Biochem. / Vol. 31,1993 / No. 4 was pancreatic phospholipase A2; since phospholipases A2 possess a highly conserved protein structure (8, 9), polyclonal antibodies against the pancreatic enzyme might cross-react with structurally related" isoenzymes. Immuno-reactive proteins have been found in serum of patients with non-pancreatic malignant tumours (10) as well as in rat spleen (11). On the other hand, most phospholipases A2 have a marked tendency to bind to proteins and surfaces in an unspecific manner (3, 12, 13), so that antibodyindependent binding artifacts may occur. The present article describes a practicable combination of activity measurements

Journal

Clinical Chemistry and Laboratory Medicinede Gruyter

Published: Jan 1, 1993

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