| Literature DB >> 17764969 |
A M Guzman-Partida1, O Jatomea-Fino, M R Robles-Burgueño, M Ortega-Nieblas, L Vazquez-Moreno.
Abstract
Alpha amylase inhibitor from Palo Fierro seeds (alphaAI-PF) was purified using affinity chromatography on a fetuin-fractogel column followed by anionic exchange chromatography. AlphaAI-PF has a molecular mass of 77kDa with two subunits (15.8 and 17.4 kDa), it is nonglycosylated and has pI of 4.7. AlphaAI-PF inhibited porcine pancreatic alpha-amylase (PPA) (1,4-alpha-D-glucan glucanohydrolase; EC 3.2.1.1), but was almost devoid of inhibitory activity on alpha-amylase extracts from Zabrotes subfasciatus (ZSA). Analysis of alphaAI-PF peptides showed a high homology to alphaAI-1 from Phaseolus vulgaris that also inhibits PPA.Entities:
Mesh：
Substances：
Year: 2007 PMID： 17764969 DOI： 10.1016/j.plaphy.2007.07.002
Source DB: PubMed Journal: Plant Physiol Biochem ISSN： 0981-9428 Impact factor: 4.270