Abstract
Isoforms of porcine pancreatic phospholipase A 2 (PLA 2) can be differentially regulated by heparin. The major isoform of PLA 2 can bind to heparin-Affigel and its catalytic activity can be inhibited by heparin. The interaction between this PLA 2 isoform and heparin does not require calcium ion or a functional active site. The sensitivity to heparin inhibition depends on the pH, with optimum sensitivity at pH 5–7 and greatly diminished sensitivity as the pH is increased from 7 to 10. A minor isoform of porcine pancreatic PLA 2 cannot bind to heparin and is resistant to heparin inhibition. The resistant isoform appears to be iso-pig PLA 2. Heparin affinity chromatography therefore offers a convenient route to the isolation of structurally and functionally distinct classes of PLA 2 enzymes. The existence of classes of PLA 2 that can be differentially regulated by heparin may have important physiological consequences.
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