Characterization of alpha-amylase inhibitor from Palo Fierro seeds.
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.
Guzman-Partida
A M
AM
Centro de Investigacion en Alimentacion y Desarrollo, A.C., Ciencia de los Alimentos, Apartado Postal 1735, 83000 Hermosillo, Sonora, Mexico.
Jatomea-Fino
O
O
Robles-Burgueño
M R
MR
Ortega-Nieblas
M
M
Vazquez-Moreno
L
L
D000595:Amino Acid Sequence; D004305:Dose-Response Relationship, Drug; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D012639:Seeds / Q000737:chemistry*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D000516:alpha-Amylases