Multiple isoforms of starch branching enzyme-I in wheat: lack of the major SBE-I isoform does not alter starch phenotype
Citations Over TimeTop 15% of 2004 papers
Abstract
The role of starch branching enzyme-I (SBE-I) in determining starch structure in the endosperm has been investigated. Null mutations of SBE-I at the A, B and D genomes of wheat were identified in Australian wheat varieties by immunoblotting. By combining individual null mutations at the B and D genomes through hybridisation, a double-null mutant wheat, which lacks the B and D isoforms of SBE-I, was developed. Wheat mutants lacking all the three isoforms of SBE-I were generated from a doubled haploid progeny of a cross between the BD double-null mutant line and a Chinese Spring (CS) deletion line lacking the A genome isoform. Comparison of starch from this mutant wheat to that from wild type revealed no substantial alteration in any of the structural or functional properties analysed. Further analysis of this triple-null mutant line revealed the presence of another residual peak of SBE-I activity, referred to as SBE-Ir, in wheat endosperm representing < 3% of the activity of SBE-I in wild type endosperm.
Related Papers
- → AMP deaminase isozymes in human tissues(1982)131 cited
- → Superoxide Dismutase Isozymes in Different Human Tissues, Their Genetic Control and Intracellular Localization(1973)76 cited
- → Human enolase isozymes: electrophoretic and biochemical evidence for three loci(1976)62 cited
- → Organ-specific distribution of isozymes of 5′-nucleotide phosphodiesterase in mouse(1990)4 cited
- STUDIES OF ISOZYMES IN THE TISSUES OF RATTUS NIVIVENTER(1997)