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Human pancreatic lipase: a glycoprotein.

A De Caro, C Figarella, J Amic

    Biochimica Et Biophysica Acta
    |February 22, 1977
    PubMed
    Summary
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    Human lipase, a glycoprotein from pancreatic juice, was purified and characterized. Two isolipases were identified, showing immunological cross-reactivity with other mammalian lipases.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Human pancreatic lipase is crucial for dietary fat digestion.
    • Understanding its structure and properties aids in comprehending fat metabolism.

    Purpose of the Study:

    • To purify and characterize human pancreatic lipase.
    • To investigate its glycoprotein nature and identify potential isolipases.
    • To examine immunological relationships with other mammalian lipases.

    Main Methods:

    • Purification of human lipase from pancreatic juice.
    • Molecular weight determination and N-terminal residue analysis.
    • Glycoprotein composition analysis (glucosamine, mannose, fucose, galactose, glucose).
    • Separation of isolipases using polyacrylamide gel electrophoresis (PAGE).

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  • Isoelectric point determination.
  • Immunological cross-reactivity assays.

    • Main Results:

    • Human lipase purified from pancreatic juice has a molecular weight of 48,000 Da with lysine as the N-terminal residue.
    • The enzyme is a glycoprotein, with specific molar ratios of constituent sugars (glucosamine, mannose, fucose, galactose, glucose).
    • Two distinct isolipases were separated by PAGE, with isoelectric points of 5.80 and 5.85, both confirmed as glycoproteins.
    • Significant immunological cross-reactions were observed between human lipase and lipases from porcine, bovine, ovine, canine, and rat species.

    Conclusions:

    • Human pancreatic lipase is a glycoprotein with a defined molecular weight and N-terminal amino acid.
    • The presence of two isolipases suggests potential functional or regulatory differences.
    • The immunological similarities indicate conserved structural features among mammalian lipases.