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H Zühlke1, K -D. Kohnert, M Ziegler

  • 1Zentralinstitut für Diabetes "Gerhardt Katsch", Bereich experimentelle Diabetesforschung, Karlsburg bei, Greifswald, DDR

FEBS Letters
|May 20, 1971
PubMed
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Researchers isolated a high molecular weight component from bovine insulin using gel filtration. This component showed reduced biological and immunological activity, indicating it is not pure insulin.

Area of Science:

  • Biochemistry
  • Endocrinology
  • Protein Chemistry

Background:

  • Bovine insulin is a crucial protein hormone regulating blood glucose.
  • Characterizing insulin components is vital for understanding its function and potential therapeutic applications.

Purpose of the Study:

  • To isolate and characterize a high molecular weight component from commercial bovine insulin.
  • To assess the biological and immunological activity of the isolated component.

Main Methods:

  • Gel filtration chromatography using Sephadex G 50.
  • Ultracentrifugation to determine molecular weight.
  • Assays for biological and immunological activity, including precipitation with antibodies and incubation with trypsin.

Main Results:

Related Experiment Videos

  • A high molecular weight component was successfully isolated from bovine insulin.
  • The component exhibited significantly lower biological and immunological activity compared to native insulin.
  • Ultracentrifugation revealed a molecular weight of 28,500 for the component.
  • The component did not show altered activity after trypsin incubation.
  • Precipitation with bovine insulin antibodies confirmed the presence of insulin-like proteins, suggesting heterogeneity.

Conclusions:

  • The isolated high molecular weight component is not homogenous insulin.
  • This component possesses altered biological and immunological properties compared to native bovine insulin.
  • Further investigation is needed to identify the exact nature of the insulin-like proteins within the component.