Introduction Serum phospholipase A2 (EC 126.96.36.199) 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
Clinical Chemistry and Laboratory Medicine – de Gruyter
Published: Jan 1, 1993
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