Effect of solubilization on the binding activity of a G-protein from the mandibular organ of the lobster Homarus americanus (Nephropidae, Decapoda)

A 50% aqueous EtOH extract of Aglaonema treubii found to potently inhibit α-glucosidase was subjected to various ion-exchange column chromatographic steps to give 2(R),5(R)-bis(hydroxymethyl)-3(R),4(R)-dihydroxypyrrolidine (1), α-homonojirimycin (2), β-homonojirimycin (3), α-homomannojirimycin (4), β-homomannojirimycin (5), α-3,4-di-epi-homonojirimycin (6), 7-O-β-d-glucopyranosyl-α-homonojirimycin (7), and 5-O-α-d-galactopyranosyl-α-homonojirimycin (8). Compounds 1 and 2 are known inhibitors of various α-glucosidases. Compounds 6 and 8 are new natural products. Compounds 3−5 and 7 have been chemically synthesized previously, but this is the first report of their natural occurrence.

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Homonojirimycin Isomers and Glycosides from Aglaonema treubii

Asano¹,

Nishida²,

Kizu³

et al. 1997

J. Nat. Prod.

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Effect of solubilization on the binding activity of a G-protein from the mandibular organ of the lobster Homarus americanus (Nephropidae, Decapoda)

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Homonojirimycin Isomers and Glycosides from Aglaonema treubii

Homonojirimycin Isomers and Glycosides from Aglaonema treubii

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