Abstract
Evidence has been sought on the possible existence of multiple forms of the enzyme controlled by the Li locus in white clover. During purification of enzyme from LiLi plants, there was no separation of activities against the β-glucosides, p-nitrophenyl β-d-glucoside, salicin, and linamarin-lotaustralin, and the β-galactoside, p-nitrophenyl β-d-galactoside. In addition, tests on mixtures of these four substrates provided no evidence for the existence of more than one enzyme. Immunological tests have shown that plants homozygous for the recessive li allele do not contain an enzymatically inactive protein, antigenically related to the normal enzyme. This suggests that li alleles either specify a low-activity immunologically altered protein or control the synthesis of very low levels of normal enzyme.
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Hughes, M.A., Maher, E.P. Studies on the nature of the Li locus in Trifolium repens L. I. Purification and properties of the enzyme components. Biochem Genet 8, 1–12 (1973). https://doi.org/10.1007/BF00485552
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DOI: https://doi.org/10.1007/BF00485552