Studies on the active center of pancreatic amylase - I. Binding of β-cyclodextrin

Susan Móra, I. Simon, Pál Elödi

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

1. The fact that β-cyclodextrin inhibits the hydrolysis of amylase suggests that β-cyclodextrin binds to the active center of pancreatic α-amylase EC 3.2.1.1. 2. As shown by preparative ultracentrifugation, amylase binds specifically three moles of β-cyclodextrin per mole enzyme and the binding can be characterized by a single dissociation constant. 3. The dissociation constant of amylase-β-cyclodextrin complex determined by kinetic methods is KI = 200 μm, which agrees well with the value KD = 140 μm, determined by preparative ultracentrifugation, and with the value KS = 220 μm arrived at by spectrophotometric titration. 4. Solvent perturbation studies indicate that out of the three bound β-cyclodextrin molecules only one interacts with a tryptophyl side chain of amylase.

Original languageEnglish
Pages (from-to)205-209
Number of pages5
JournalMolecular and Cellular Biochemistry
Volume4
Issue number3
DOIs
Publication statusPublished - Oct 1974

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Cyclodextrins
Amylases
Ultracentrifugation
Titration
Hydrolysis
Molecules
Kinetics
Enzymes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

Cite this

Studies on the active center of pancreatic amylase - I. Binding of β-cyclodextrin. / Móra, Susan; Simon, I.; Elödi, Pál.

In: Molecular and Cellular Biochemistry, Vol. 4, No. 3, 10.1974, p. 205-209.

Research output: Contribution to journalArticle

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