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• W64229998 abstract "Zein is the major storage protein (50-60% of the total protein) fraction in the maize endosperm, and it consists of a group of highly hydrophobic proteins. during seed development zein is deposited in distinct membrane-bound subcellular compartments called protein bodies (Wolf et al. 1969, Larkins and Hurkman 1978). The function of zein is thought to be that of a nitrogen source during germination and early seedling growth, and of a nitrogen sink during seed development (Tsai et al. 1978,1980). Zein proteins are completely devoid of two essential amino acids (lysine and tryptophan) and are therefore primarily responsible for the low protein nutritional quality of maize meal and its products. Consequently, there has been continuing interest in improving the nutritional quality of maize and other cereals, as they are major staples providingmost of the calories and protein directly or indirectly for nearly 90% of the worid’s population. The realization of this goal will be dependent upon a thorough knowledge of the structure, function, and regulation of the synthesis and sequestering of zein proteins, as well as prolamins from other cereals. Zein is commonly extracted with 60-70% alcohol solutions and can be separated into three distinct fractions by differential solubility fractionation (Esen 1986). These three fractions have been designated as α-zein (23.8 and 26.7 kDa zeins), β-zein (17 and 18 kDa zeins), and γ-zein (27 kDa zein) Esen 1987). There is also minor 10 kDa zein polypeptide, δ-zein, which exhibits solubility characteristics similar to those of α-zeins. Prat et al. (1987) deduced the complete primary structure of the 18 kDa polypeptide and showed that it shared over 70% sequence similarity with γ-zein (27 kDa) when tandemly repeated hexapeptide region of γ-zein is excluded from sequence comparison. In view of these data, the nomenclature system of Esen (1987) has recently been modified (Esen 1990). In the modified system (Fig. 1), the 18 kDa polypeptide has been removed from β-zein class and designated as γ-zein2, while the 27 kDa polypeptide (formeriy γ-zein) is now referred to as γ-zein1,. Of the different zein fractions, α-zein is the most abundant (75-80% of the total zein) and includes polypeptides with mw 23.8 to 26.7 kDa encoded by members of a multigene family (Parks et al. 1980; Marks et al. 1985). β-Zein includes a methionine-rich polypeptide of 17 kDa and constitutes up to 10% of the total" @default.
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• W64229998 date "1994-01-01" @default.
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• W64229998 title "Synthetic Peptides and Antipeptide Antibodies in Studying Zein Structure and Fingerprinting Maize Genotypes" @default.
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• W64229998 doi "https://doi.org/10.1007/978-3-642-57968-4_37" @default.
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