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Clinical Chemistry 29: 1772-1776, 1983;
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Clinical Chemistry, Vol 29, 1772-1776, Copyright © 1983 by American Association for Clinical Chemistry

Purification and characterization of human pancreatic phospholipase A2

JU Eskola, TJ Nevalainen and HJ Aho

We purified human pancreatic phospholipase A2 from postmortem pancreatic tissue by elution of the semi-purified enzyme on CM-Sephadex C-25 with a linear NaCl gradient at pH 6.0. The enzyme appeared as a single polypeptide chain with an isoelectric point of 9.2 +/- 0.1. The relative molecular mass of the enzyme was estimated to be 15 800 +/- 1000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The enzyme is resistant to heating and to a 25 g/L concentration of sodium dodecyl sulfate. It is inhibited by Ca2+ ions in the presence of ovolecithin and deoxycholate. By immunohistochemical methods we showed the enzyme to be localized in the apical zymogen granule portion of pancreatic acinar cells.


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


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 J BiochemHome page
A. A. Sattar and R. Haque
Cytosolic PLA2 in Zymogen Granule Fusion and Amylase Release: Inhibition of GTP-induced Fusion by Arachidonyl Trifluoromethyl Ketone Points to cPLA2 in G-Protein-mediated Secretory Vesicle Fusion
J. Biochem., January 1, 2007; 141(1): 77 - 84.
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Copyright © 1983 by the American Association for Clinical Chemistry.