Related Experiment Videos
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
Summary
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.