Characterization and function of pig intestinal sucrase‐isomaltase and its separate subunits

Ignacio R. RODRIGUEZ, Francois R. TARAVEL, William J. WHELAN

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

1. Papain‐solubilized pig intestinal sucrase‐isomaltase was purified to homogeneity in a four‐step process with a yield of 50%. 2. The substrate specificities of the two enzyme activities were studied together and separately after inactivation or inhibition of one of the activities. 3. Michaelis constants, maximum velocities and time courses of hydrolysis of several substrates, in particular α‐limit dextrins, were used to characterize this complex of α‐glucosidases. 4. The participation of the enzyme complex in the hydrolysis of α‐limit dextrins and more generally in pathways for starch breakdown in the pig digestive tract is examined and discussed.

Original languageEnglish (US)
Pages (from-to)575-582
Number of pages8
JournalEuropean Journal of Biochemistry
Volume143
Issue number3
DOIs
StatePublished - Sep 1984

ASJC Scopus subject areas

  • Biochemistry

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