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Plant Physiol Biochem. 2007 Sep;45(9):711-5. Epub 2007 Jul 22.

Characterization of alpha-amylase inhibitor from Palo Fierro seeds.

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1
Centro de Investigacion en Alimentacion y Desarrollo, A.C., Ciencia de los Alimentos, Apartado Postal 1735, 83000 Hermosillo, Sonora, Mexico.

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.

PMID:
17764969
DOI:
10.1016/j.plaphy.2007.07.002
[Indexed for MEDLINE]
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