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Dep. of Agronomy, Univ. of Kentucky, Lexington, KY 40546
Dep. of Agronomy and Plant Genetics, Univ. of Minnesota, St. Paul, MN 55108
* Corresponding author.
Three soybean [Glycine max (L) Merr.] seed lipoxygenase isozymes, involved in generating products which contribute to undesirable flavors in processed protein products, have been characterized genetically. The objective of this study was to determine the inheritance of an alternate lipoxygenase-1 allozyme, which has a more acidic isoelectric point than the normal allozyme (pI 5.79 vs. pI 5.85 for the normal allozyme). This alternate allozyme was originally seen in soybean strains L2-3 and PI 86023, which are null for lipoxygenase-2, genotype lx2 lx2. A similar alternate allozyme was subsequently seen in McCall. The 1:2:1 F2 segregation ratios from several crosses of "normal" allozyme x alternate allozyme parents indicated codominant inheritance of the two allozymes. The gene symbol Lxb1 is assigned to the allozyme with pI 5.79, and the gene symbol for the allozyme with pI 5.85 becomes Lxa1 This gives an allelic series at the lipoxygenase-1 locus Lxa1, Lxb1, and lx1. The lx1 and lx2 loci are very tightly linked. Crosses between Lxa1 Lxa1 Lx2Lx2 and Lxb1 Lxb1 lx2lx2 genotypes would be designed to incorporate the lx2lx2 genotype into cultivars with improved protein flavor attributes for soyfood products. while phenotypes of Lx2Lx2 and lx2lx2 genotypes are indistinguishable in terms of lipoxygenase-2, the presence of two electrophoretic bands for lipoxygenase-1 (Lxa1 Lxb1) when the lipoxygenase-2 locus is also heterozygous makes it possible to identify individuals with the recessive lx2 allele. The selection of heterozygotes can reduce the time needed to backcross the lx2 allele.
Received for publication September 3, 1992.
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