Characterization of a phospholipase A2 in human serum
Hoffmann, G.E.; Schneider, E.; Brand, K.; Kozumplik, V.; Fateh-Moghadam, S.
European Journal of Clinical Chemistry and Clinical Biochemistry 30(3): 111-117
1992
ISSN/ISBN: 0939-4974 PMID: 1599975 Document Number: 397075
Elevated catalytic activities of serum phospholipase A2 were measured in patients with inflammatory diseases. In contrast to human pancreatic phospholipase A2, the enzyme in serum of patients with non-pancreatic diseases was rather heat labile and showed a broad pH-optimum in the neutral range. Molecular sieving experiments revealed the existence of macro-molecular forms of the enzyme in serum which were cleaved into monomers of M(r) 14,000 in the presence of high salt concentrations. More than 100-fold purification was achieved by gel filtration chromatography on Sephadex G-100 in the presence of 2 mol/l KCl. Whether this serum phospholipase A2 and a secretory liver and platelet isoenzyme are identical remains to be established.