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, 146 (2), 199-202

Uridinediphosphate-glucose: Isovitexin 7-O-glucosyltransferase From Barley Protoplasts: Subcellular Localization

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Uridinediphosphate-glucose: Isovitexin 7-O-glucosyltransferase From Barley Protoplasts: Subcellular Localization

D E Blume et al. Planta.

Abstract

Protoplasts isolated from 6-d-old primary leaves of barley (Hordeum vulgare L.) contain an enzyme which transfers the glucosyl moiety of uridine-diphosphateglucose to isovitexin, resulting in the formation of saponarin, the major flavonoid of barley. Purified chloroplasts isolated from protoplasts contained less than 2% of the total glucosyltransferase activity. These chloroplasts were 97% intact, based on ribulose-bisphosphate-carboxylase activity. Similarly low levels of glucosyltransferase activity were found in mitochondria and microbody or microsomal preparations from protoplasts. The soluble fraction (cytosol) contained at least 93% of the isovitexin 7-O-glucosyltransferase activity.

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Cited by 4 PubMed Central articles

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