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Gastric proteases in the human infant

M J Henschel1, M J Newport, V Parmar

  • 1National Institute for Research in Dairying, Shinfield, Reading, Berks, UK.

Biology of the Neonate
|January 1, 1987
PubMed

Insights

Human infants may secrete chymosin, an enzyme typically found in calves. Gastric juice analysis revealed chymosin-like enzymes in premature infants, suggesting species-specific variations in protease development.

Area of Science:

  • Biochemistry
  • Gastroenterology
  • Pediatrics

Background:

  • Gastric proteases play a crucial role in infant digestion.
  • Chymosin is a primary protease in suckling mammals, aiding milk digestion.
  • Pepsin is another significant gastric protease, with various forms identified.

Purpose of the Study:

  • To investigate the presence and types of proteases in the gastric juice of premature infants.
  • To compare infant gastric proteases with known enzymes like calf chymosin and adult human pepsin.
  • To determine if human infants secrete chymosin.

Main Methods:

  • Electrophoretic separation of proteases from infant gastric juice.
  • Comparison of electrophoretic mobilities with calf chymosin and pig pepsin A.
  • Single radial immunodiffusion using calf anti-chymosin serum on infant gastric juice samples.

Main Results:

  • Gastric juice from premature infants showed varied protease profiles: some predominantly chymosin-like, others adult-like pepsin, and some a mixture.
  • Electrophoresis identified two pepsin components, likely pepsin A and pepsin C.
  • Immunodiffusion confirmed the presence of chymosin-like antigens in samples from 17 infants.

Conclusions:

  • Human infants can secrete chymosin, indicating a potential role in early digestion.
  • Observed differences in enzyme activity between electrophoresis and immunodiffusion may be due to antiserum cross-reactivity.
  • Further research is needed to fully understand the functional significance and developmental patterns of gastric proteases in infants.

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