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An analysis of soluble starch synthase isozymes from the developing grains of normal and shx cv. Bomi barley (Hordeum vulgare)
Authors:Janna Tyynelä  Alan H Schulman
Institution:Dept of Medical Chemistry, Univ. of Helsinki and A. H. Schulman (corresponding author);Inst. of Biotechnology, PO Box 45, FIN-00014 Univ. of Helsinki, Finland.
Abstract:Soluble starch synthase (SSS, EC 2.4.1.21) catalyzes formation of the α-1,4 bonds of amylopectin. It occurs in multiple isozymes which are either type I, primer-independent in the presence of citrate, or type II. always primer-dependent. To analyze the enzyme. a sensitive native gel assay was developed, monitoring ADP-14C]glucose incorporation into insoluble α-glucan in the presence of either sodium citrate or glycogen primer or both. Using this system, we observed multiple type I and type II forms in developing grains of barley ( Hordeum vulgare L.) cv. Bomi, the relative activities of which vary with seed development. At least one form comigrates in native gels with starch branching enzyme. Assays of the shx mutant, which is severely reduced in starch accumulation and in type I SSS activity, indicate that one type I isozyme becomes primer-dependent.
Keywords:Barley  endosperm              Hordeum vulgare            isozymes  native gel assay              shx            mutant  soluble starch synthase  starch branching enzyme
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