Abstract
The granule-bound starch-synthases from normal and waxy maize kernels have been solubilized, partially purified, and characterized. Two broad categories of starch synthases were revealed with representatives in the soluble phase and also on granules from both normal and waxy maize though the activity associated with granules from waxy was small. Data for native molecular weights, kinetic parameters, and immunological relatedness are used to demonstrate that the granule-bound isozymes from normal maize are different from the soluble enzymes. These distinct granule-bound enzymes are missing in waxy maize granules and a further novel form of starch synthase is revealed. These findings are discussed in relation to the type of starch produced in tissue affected by the waxy mutation.
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Selected References
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- Echt C. S., Schwartz D. Evidence for the Inclusion of Controlling Elements within the Structural Gene at the Waxy Locus in Maize. Genetics. 1981 Oct;99(2):275–284. doi: 10.1093/genetics/99.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Frydman R. B., Cardini C. E. Studies on the biosynthesis of starch. II. Some properties of the adenosine diphosphate glucose:starch glucosyltransferase bound to the starch granule. J Biol Chem. 1967 Jan 25;242(2):312–317. [PubMed] [Google Scholar]
- Hawker J. S., Ozbun J. L., Ozaki H., Greenberg E., Preiss J. Interaction of spinach leaf adenosine diphosphate glucose alpha-1,4-glucan alpha-4-glucosyl transferase and alpha-1,4-glucan, alpha-1,4-glucan-6-glycosyl transferase in synthesis of branched alpha-glucan. Arch Biochem Biophys. 1974 Feb;160(2):530–551. doi: 10.1016/0003-9861(74)90430-5. [DOI] [PubMed] [Google Scholar]
- Holmes E., Preiss J. Characterization of Escherichia coli B glycogen synthase enzymatic reactions and products. Arch Biochem Biophys. 1979 Sep;196(2):436–448. doi: 10.1016/0003-9861(79)90295-9. [DOI] [PubMed] [Google Scholar]
- MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
- Macdonald F. D., Preiss J. Solubilization of the starch-granule-bound starch synthase of normal maize kernels. Plant Physiol. 1983 Sep;73(1):175–178. doi: 10.1104/pp.73.1.175. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nelson O. E., Chourey P. S., Chang M. T. Nucleoside Diphosphate Sugar-Starch Glucosyl Transferase Activity of wx Starch Granules. Plant Physiol. 1978 Sep;62(3):383–386. doi: 10.1104/pp.62.3.383. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ozbun J. L., Hawker J. S., Preiss J. Adenosine diphosphoglucose-starch glucosyltransferases from developing kernels of waxy maize. Plant Physiol. 1971 Dec;48(6):765–769. doi: 10.1104/pp.48.6.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Polacheck I., Cabib E. A simple procedure for protein determination by the Lowry method in dilute solutions and in the presence of interfering substances. Anal Biochem. 1981 Nov 1;117(2):311–314. doi: 10.1016/0003-2697(81)90784-3. [DOI] [PubMed] [Google Scholar]
- Pollock C., Preiss J. The citrate-stimulated starch synthase of starchy maize kernels: purification and properties. Arch Biochem Biophys. 1980 Oct 15;204(2):578–588. doi: 10.1016/0003-9861(80)90070-3. [DOI] [PubMed] [Google Scholar]
- Shaltiel S., Er-El Z. Hydrophobic chromatography: use for purification of glycogen synthetase. Proc Natl Acad Sci U S A. 1973 Mar;70(3):778–781. doi: 10.1073/pnas.70.3.778. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shure M., Wessler S., Fedoroff N. Molecular identification and isolation of the Waxy locus in maize. Cell. 1983 Nov;35(1):225–233. doi: 10.1016/0092-8674(83)90225-8. [DOI] [PubMed] [Google Scholar]