Phaseolin: Nucleotide Sequence Explains Molecular Weight and Charge Heterogeneity of a Small Multigene Family and also Assists Vector Construction for Gene Expression in Alien Tissue
It is now well established that the seed storage proteins of major crop species are encoded as families of closely related genes. Similarities and divergencies are being defined at the levels of protein structure, amino acid sequence, and nucleotide sequence, (see Brown, Ersland, and Hall, 1982, and Ersland et al., 1983 for reviews). Phaseolin, the major storage protein of the French bean (Phaseolus vulgaris L.) can be separated into a group of about ten closely related polypeptides by two-dimensional PAGE. Analysis of some 150 cultivars yielded only three different patterns, characterized as T (Tendergreen), S (Sanilac) and C (Contender) types (Brown et al., 1981a). The component polypeptides range in apparent molecular weight from 45 to 51 kd, and in isoelectric point from pH 5.6–5.8 (Fig. 1). The T, S and C patterns contained 5, 8 and 8 polypeptides respectively.
KeywordsHydrolysis Corn Mercury Bromide Electrophoresis
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