COMPETITIVE INHIBITION OF HISTOCHEMICAL SUBSTRATES FOR GLYCOSIDASES
Abstract
Competitive inhibition of glycosidases in the rat jejunum was studied using four halogen-substituted indolyl substrates: 5-bromo-4-chloroindol-3-yl- beta-D- galactopyranoside, 5-bromo-4-chloroindol-3-yl-beta-D-fucopyranoside, 5- bromo-4- chloroindol-3-yl-beta-D-glucopyranoside, and 5-bromo-4-chloroindol-3- ylbeta-D glucopyruroniside. These substrates have identical indolyl moieties and differ only in the substitution and/or configuration of the glycon. Inhibition of enzyme activity was studied with sugars and sugar derivatives whose structure was analogous to that of the glycosides. In general, inhibition was noted when the substrate and inhibitor were derived from the same sugar. Aldonolactones were the strongest inhibitors, and, from the limited data, carboxyl substituents appeared to be more important than other end groups or the configuration of the pyranoside ring.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1967
- Accession Number
- AD0821511
Entities
People
- John R. Esterly