Preliminary X-ray investigation of a bifunctional inhibitor from Indian finger millet (ragi)

J Mol Biol. 1991 Nov 5;222(1):1-2. doi: 10.1016/0022-2836(91)90728-o.

Abstract

A bifunctional alpha-amylase/trypsin inhibitor that has two binding sites has been purified from ragi. The inhibitor has been crystallized from its ammonium sulphate solution by the vapour diffusion method. The crystals belong to the orthogonal space group P2(1)2(1)2(1) with unit cell dimensions a = 30.49 A, b = 56.30 A, c = 73.65 A and Z = 4.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amylases / antagonists & inhibitors*
  • Binding Sites
  • Cross-Linking Reagents
  • Poaceae / chemistry*
  • Trypsin Inhibitors / chemistry*
  • Trypsin Inhibitors / isolation & purification
  • X-Ray Diffraction

Substances

  • Cross-Linking Reagents
  • Trypsin Inhibitors
  • Amylases