Classic Papers by J.A. Callow (Eds.)

By J.A. Callow (Eds.)

Articles during this vintage Papers quantity are rewritten, up-dated and prolonged models of papers released in prior volumes of Advances in Botanical study, selected a result of excessive quotation of the unique papers and the rise of data within the box this present day. Boulter and Croy talk about the constitution and biosynthesis of legume seed garage proteins, a space that has been revolutionized in recent times by Read more...

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1990). The precise roles which the hormones, cytokinin, auxin, abscisic acid (ABA) play in seed development are still largely unknown (McCarty, 1995). Only in the case of ABA has a direct involvement of a hormone with regulation of storage protein deposition been suggested. Thus in some legume species, but not others, the behaviour of in vitro cultures of wild-type embryos and that of certain mutants has shown that ABA can prolong the synthesis of storage proteins, and delay precocious germination.

1980b, 1982, 1984b). Subsequent legumin cDNA and gene sequencing proved this to be the 26 D. BOULTER & R. R. CROY fundamental structure of all legumins. Two-dimensional gel “diagonal” methods, in which electrophoresis is performed under denaturing conditions in one direction in the absence of a reducing agent and then in the other direction, 90” to the first, after reduction, allow visualization of the legumin partners in acidic and basic subunit pairs. However, there are only a few cases where individual acidic and basic subunits have been isolated and sequenced.

1993) and only two or three legumin genes, suggesting a correlation between number of genes in the storage gene family and genome size. E. , 1969). Although purification techniques and the resolution of two-dimensional tryptic digests were not fully adequate, this work did provide a suggestion of their similarity. As DNA and protein sequence data became available, Argos et al. (1985) used these data and secondary structure predictions to show that the C-terminal domain of vicilin subunits and the basic chain of legumins share a greater degree of similarity than that found from a comparison of the N-terminal domain of vicilin and the acidic chain of legumin.

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