Complete Sequence, Subunit Structure, and Complexes with Pancreatic -Amylase of an -Amylase Inhibitor from Phaseolus vulgaris White Kidney Beans

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Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris.

Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of alpha-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal alpha-amylases, having no activity towards...

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Purification and Properties of Phaseolamin, an Inhibitor of ar-Amylase, from the Kidney Bean, Phaseohs vulgaris

Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of a-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal a-amylases, having no activity towards the cor...

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Heterologous expression of an α-amylase inhibitor from common bean (Phaseolus vulgaris) in Kluyveromyces lactis and Saccharomyces cerevisiae

BACKGROUND Phaseolamin or α-amylase inhibitor 1 (αAI) is a glycoprotein from common beans (Phaseolus vulgaris L.) that inhibits some insect and mammalian α-amylases. Several clinical studies support the beneficial use of bean αAI for control of diabetes and obesity. Commercial extracts of P. vulgaris are available but their efficacy is still under question, mainly because some of these extracts...

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Activation of bean (Phaseolus vulgaris) alpha-amylase inhibitor requires proteolytic processing of the proprotein.

Seeds of the common bean (Phaseolus vulgaris) contain a plant defense protein that inhibits the alpha-amylases of mammals and insects. This alpha-amylase inhibitor (alpha AI) is synthesized as a proprotein on the endoplasmic reticulum and is proteolytically processed after arrival in the protein storage vacuoles to polypeptides of relative molecular weight (M(r)) 15,000 to 18,000. We report two...

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Activity changes in cranberry bean (Phaseolus vulgaris) alpha-amylase inhibitor by chemical modification and enzymatic digestion.

An alpha-amylase inhibitor was prepared from cranberry bean (Phaseolus vulgaris). The alpha-amylase inhibitor was composed of three different subunits not linked by disulfide bridges and only one of them contained carbohydrate. Although the inhibitor was stable at pH 3 to 7, it was heat labile at pH 3 and 5. Chemical modification of the amino groups and the guanido groups in cranberry bean alph...

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ژورنال

عنوان ژورنال: Journal of Biochemistry

سال: 1996

ISSN: 0021-924X

DOI: 10.1093/oxfordjournals.jbchem.a021381