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Esterolytic activity of blood serum in infants with hypertrophic pyloric stenosis

Journal of Clinical Chemistry and Clinical Biochemistry. Zeitschrift Fur Klinische Chemie Und Klinische Biochemie
|May 1, 1979
PubMed

Insights

Infants with hypertrophic pyloric stenosis show elevated serum arylesterase activity, specifically hydrolyzing p-nitrophenyl propionate faster than other esters. This contrasts with healthy infants where hydrolysis rates are similar across substrates.

Area of Science:

  • Biochemistry
  • Pediatric Gastroenterology
  • Enzymology

Background:

  • Hypertrophic pyloric stenosis (HPS) is a common infant condition affecting the stomach outlet.
  • Serum esterase activity, particularly arylesterase, may play a role in HPS pathogenesis.
  • Understanding enzyme kinetics in HPS is crucial for diagnostic and therapeutic insights.

Purpose of the Study:

  • To investigate and compare serum esterolytic activity in infants with HPS versus healthy controls.
  • To determine the specific esterase substrates most affected in infants diagnosed with HPS.
  • To elucidate the role of arylesterase in the physiological changes associated with hypertrophic pyloric stenosis.

Main Methods:

  • Serum samples were collected from infants diagnosed with HPS and from a healthy control group.
  • The hydrolysis rates of p-nitrophenyl esters of acetic, propionic, and butyric acid were measured.
  • Enzyme kinetics were analyzed to quantify esterolytic activity using specific substrates for arylesterase (EC. 3.1.1.2).

Main Results:

  • Infants with HPS exhibited significantly higher hydrolysis rates for p-nitrophenyl propionate compared to acetate and butyrate.
  • In healthy control infants, hydrolysis rates for all three substrates were similar.
  • The overall esterolytic activity, particularly for propionate, was significantly elevated in the HPS group compared to controls.

Conclusions:

  • Serum arylesterase activity is significantly altered in infants with hypertrophic pyloric stenosis.
  • The preferential hydrolysis of p-nitrophenyl propionate suggests a specific enzymatic change associated with HPS.
  • These findings may offer potential biomarkers for diagnosing or understanding the pathophysiology of HPS.

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