Interest of Using a Purified, Stable and Commutable Preparation of Human Pancreatic Lipase in Indirect Assays

@inproceedings{Lessinger1992InterestOU,
  title={Interest of Using a Purified, Stable and Commutable Preparation of Human Pancreatic Lipase in Indirect Assays},
  author={Jean Marc Lessinger and Anna Tavridou and Pantelis Arzoglou and Georges F{\'e}rard},
  year={1992}
}
Abstract Human lipase has been purified from pancreatic juice. The procedure involved ammonium sulphate fractionation, anion exchange chromatography, preparative isoelectric focusing, gel filtration and cation exchange chromatography. Apparent molecular weight and pI were found to be 48 kDa and 7.5 respectively. Purified enzyme supplemented with buffered human albumin 40 g/1 and sodium azide 1 g/1 was stable in solution at 4°C for at least 200 days. The effects of bile salts, colipase and ionic… CONTINUE READING

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Plasma pancreatic lipase activity: from analytical specificity to clinical efficiency for the diagnosis of acute pancreatitis.

  • European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies
  • 1994

Transferability of Lipase Titrimetric Assays: Deductions from an Interlaboratory Study

  • European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies
  • 1994
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