Isolation and characterization of the storage protein of yam tubers (Dioscorea rotundata)

Author(s): Harvey PJ, Boulter D

Abstract

The major proteins of the yam tuber, which were identified as storage proteins by virtue of their abundance (ca 85 % of the total protein content), amino acid composition (high in amide content) and cellular location within the tuber, were isolated by ion-exchange chromatography and characterized using, in particular, polyacrylamide gel techniques. They consist principally of subunits of one size, apparent MW 31 000, and N-terminal amino acid glutamine/glutamic acid, of which there are a number of charge isomers; these usually contain one intra-chain disulphide bond. The subunits associated into polymers depending on the protein concentration, pH value and ionic strength of the milieu and, therefore, a value for the MW of the native protein(s) is not given. The storage proteins are not glycoproteins. They are intracellularly located as protein ’aggregates‘ within cellular protein vacuoles, and also within the cytoplasm.

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