Studies on the active center of pancreatic amylase - II. Small angle X-ray scattering investigations

István Simon, Susan Móra, Pál Elödi

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

1. The radius of gyration of α-amylase is 26.9 Å, as found by means of small angle X-ray scattering. This value decreases by 0.5 Å if amylase binds three moles of β-cyclodextrin per mole enzyme. 2. In case of partial saturation, the solution contains only saturated amylase-cyclodextrin complexes (amylase/cyclodextrin molar ratio 1:3) and amylase molecules free of cyclodextrin. The binding of β-cyclodextrin follows the all-or-none mechanism. 3. The specifically bound β-cyclodextrin molecules are accommodated in a trough of the amylase molecule. The plane of bound cyclodextrin is perpendicular to the longitudinal axis of the trough. It is suggested that the helical substrate, amylose, binds in this trough, too.

Original languageEnglish
Pages (from-to)211-216
Number of pages6
JournalMolecular and Cellular Biochemistry
Volume4
Issue number3
DOIs
Publication statusPublished - Oct 1 1974

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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