Lactase-phlorizin hydrolase complex from monkey small intestine: stimulation of pillorizin hydrolase activity by organic acids

Ramaswamy , S. ; Radhakrishnan, A. N. (1973) Lactase-phlorizin hydrolase complex from monkey small intestine: stimulation of pillorizin hydrolase activity by organic acids Biochemical and Biophysical Research Communications, 54 (1). pp. 197-204. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000629...

Related URL: http://dx.doi.org/10.1016/0006-291X(73)90908-X

Abstract

Lactase-phlorizin hydrolase complex from monkey small intestine reveals a new phlorizin hydrolase activity at pH 3.3 in the presence of certain organic acids in addition to the normal activity at optimum pH 5.4. The highest stimulation (10-15 fold) was obtained with tartaric acid. Lactase activity at pH 5.3 is unaffected but its activity at pH 3.3 is inhibited by organic acids. Tartaric acid-stimulated phlorizin hydrolase activity is inhibited by a number of organic acids which have no effect on the unstimulated enzyme. Pyruvic acid inhibits the unstimulated activity as well. SO42- and Cl- ions are potent inhibitors of the tartaric acid-stimulated phlorizin hydrolase.

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