Jul 21, 1976

Insulin and glucagon degradation by the kidney. II. Characterization of the mechanisms at neutral pH

Biochimica Et Biophysica Acta
W C Duckworth


Examination of insulin and glucagon degradation by rat kidney subcellular fractions revealed that most degrading activity was localized to the 100 000 X g pellet and 100 000 X g supernatant fractions. Further characterization of the degrading activities of the 100 000 X g pellet and supernatant suggested that three types of enzymatic activity were present at neutral pH. From the cytosol an enzyme with characteristics of the insulin glucagon protease of skeletal muscle was purified. This enzyme appeared to be responsible for insulin degradation by the kidney at physiological insulin concentrations. This enzyme also contributed to glucagon degradation but was not the most active mechanism for this. In the 100 000 X g pellet at least two separate enzymatic activities were present. One of these had properties consistent with those described for glutathione insulin transhydrogenase and appeared to be responsible for insulin degradation at high insulin concentration. The other enzyme was associated with the brush border and had properties consistent with the brush border neutral protease. This enzyme appeared responsible for glucagon degradation at both low and high substrate concentrations. An apparent marked synergism between the 1...Continue Reading

  • References3
  • Citations13


  • References3
  • Citations13


Mentioned in this Paper

Glutathione-insulin transhydrogenase
Glucagon (rDNA)
Pellet Formation
Peptide Hydrolases
Brush border antigen
Proteolytic Enzyme

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