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Related Experiment Videos

Pepsin and its multiple forms in early life.

I Adamson1, A Esangbedo, A A Okolo

  • 1Department of Biochemistry, University of Benin, Benin City, Nigeria.

Biology of the Neonate
|January 1, 1988
PubMed
Summary

Pre-term infants show lower pepsin enzyme activity and acidity. Specific pepsin isoenzymes develop later in the neonatal period, impacting infant nutrition management.

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Area of Science:

  • Neonatal physiology
  • Gastrointestinal enzymology

Background:

  • Pepsin is a key gastric enzyme crucial for protein digestion.
  • Understanding pepsin development in neonates is vital for assessing nutritional needs.

Purpose of the Study:

  • To investigate pepsin activity and molecular forms in Nigerian infants.
  • To determine the developmental timeline of pepsin isoenzymes in the neonatal period.

Main Methods:

  • Analysis of total pepsin enzyme activity and acidity.
  • Ion-exchange chromatography and electrophoresis for isoenzyme resolution.

Main Results:

  • Lower total pepsin activity and acidity observed in pre-term infants compared to term and post-term infants.
  • Specific pepsin isoenzyme development was noted towards the end of the neonatal period in term infants.

Conclusions:

  • Differential development of pepsin and its isoenzymes in neonates may influence pancreatic protease activity.
  • Findings provide a basis for evaluating gastric capacity for infant nutritional management.

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