Abstract
Summary The preparation of 14C-labelled monogalactosyl diglyceride and 3H-labelled digalactosyl diglyceride is described. Using these substrates it was confirmed that acyl galactosyl diglyceride can be formed by dismutation of monogalactosyl diglyceride or by acyl transfer from di- to monogalactosyl diglyceride. In both reactions the acyl groups of the donor molecules are transferred without positional specificity. An assay was worked out for the determination of enzymatic activity using radioactive substrates. With this assay several properties of the enzymatic activity from leaves of Vicia faba were investigated: pH-optimum, isoelectric point, dependence on substrate and detergent concentration, distribution in various organs of the plant and subcellular distribution. The enzyme was found to be a soluble protein of the cytoplasm. A partial purification and stabilization was achieved by DEAE-cellulose column chromatography.
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