| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2016697 | Plant Physiology and Biochemistry | 2007 | 5 Pages |
Abstract
Alpha amylase inhibitor from Palo Fierro seeds (αAI-PF) was purified using affinity chromatography on a fetuin-fractogel column followed by anionic exchange chromatography. αAI-PF has a molecular mass of 77 kDa with two subunits (15.8 and 17.4 kDa), it is nonglycosylated and has pI of 4.7. αAI-PF inhibited porcine pancreatic α-amylase (PPA) (1,4-α-d-glucan glucanohydrolase; EC 3.2.1.1), but was almost devoid of inhibitory activity on α-amylase extracts from Zabrotes subfasciatus (ZSA). Analysis of αAI-PF peptides showed a high homology to αAI-1 from Phaseolus vulgaris that also inhibits PPA.
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Authors
A.M. Guzman-Partida, O. Jatomea-Fino, M.R. Robles-Burgueño, M. Ortega-Nieblas, L. Vazquez-Moreno,