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H Zühlke1, H G. Lippmann, W Wilke

  • 1Institut für Diabetes "Gerhardt Katsch", Bereich experimentelle Diabetesforschung, Karlsburg/Greifswald, DDR

FEBS Letters
|February 16, 1970
PubMed
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Researchers purified insulin using preparative polyacrylamide electrophoresis (PADE), achieving a highly active substance. This proinsulin-free insulin demonstrated superior hypoglycemic activity in eviscerated rabbits compared to the Toronto standard.

Area of Science:

  • Biochemistry
  • Endocrinology
  • Pharmacology

Background:

  • Insulin purification is crucial for accurate therapeutic assessment.
  • Proinsulin contamination can affect insulin's biological activity and characterization.
  • Standardized methods are needed to evaluate insulin potency.

Purpose of the Study:

  • To obtain highly purified insulin free from proinsulin.
  • To characterize the N-terminal amino acids of the purified insulin.
  • To assess the hypoglycemic activity of the purified insulin using a validated animal model.

Main Methods:

  • Preparative polyacrylamide electrophoresis (PADE) was employed for insulin purification.
  • Analytical PADE was used to confirm the purity and uniformity of the insulin band.

Related Experiment Videos

  • N-terminal amino acid analysis was performed.
  • Hypoglycemic activity was evaluated in an eviscerated rabbit model.

    • Main Results:

    • Maximal purification of insulin was achieved, yielding a proinsulin-free substance.
    • The purified insulin presented as a single, uniform band on analytical PADE.
    • Glycine and phenylalanine were identified as the N-terminal amino acids.
    • The purified insulin exhibited significantly higher hypoglycemic activity than the Toronto standard.

    Conclusions:

    • Preparative polyacrylamide electrophoresis is an effective method for obtaining highly purified insulin.
    • The characterized proinsulin-free insulin demonstrates enhanced biological activity.
    • This purified insulin represents a potentially more potent therapeutic agent.