Studies in bile salt solutions. Deoxycholate stimulation of human milk lipase

  • O'Connor C
  • Wallace R
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Abstract

Stimulation of human milk lipase by deoxycholate and its taurine and glycine conjugates was demonstrated by measuring the esterolysis reaction of 4-nitrophenylacetate. The steroidal surfactants did not bind strongly to the polar substrate but they did bind effectively to a hydrophobic site on the enzyme and these bile salt-enzyme complexes were effective catalysts. These results are compared with those for stimulation of the enzyme by cholate surfactants and it has been demonstrated that the absence of a 7α-OH substituent on the steriod nucleus does not prevent stimulation of either the esterolytic or lipolytic activity of the enzyme. © 1984.

Author-supplied keywords

  • Bile salt-stimulated lipase
  • Esterase activity
  • Human milk lipase

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Authors

  • Charmian J. O'Connor

  • Robert G. Wallace

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