Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors
✍ Scribed by Hanne Frøkiaer; Lene Hørlyck; Susanne Sørensen; Hilmer Sørensen
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 808 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0022-5142
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A black gram (Vigna mungo) trypsin inhibitor (BGTI) was purified to homogeneity by ammonium sulphate precipitation, DEAE-cellulose chromatography and affinity chromatography. The homogeneity of the inhibitor was identified by polyacrylamide gel electrophoresis (PAGE), SDS-PAGE, immunodiffusion and i
Soybean trypsin inhibitor (STI) was immobilized on the agarose gel modified with spiropyran compound (spiropyran gel), and photocontrolled binding and releasing oftrypsin was examined. The STI-spiropyran gel showed reverse photochromism. Trypsin was bound on the STI-spiropyran gel in the dark and re