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          玉米蛋白,黍膠質(zhì);玉米朊;玉米醇溶蛋白 寶葉提供

          更新時間:2013-06-03點擊次數(shù):1903

          Zein is a prolamine; an alcohol-soluble protein present
          in amounts of 2.5-10% (dry basis) in corn. Zein is a
          common component used in the manufacture of
          plastics, paper coatings, adhesives, substitutes for
          shellac, laminated board, and solid color printing films.
          Zeins are the main storage proteins found in the seeds
          of maize. Following protein translation, the zeins are
          stored in the rough endoplasmic reticulum
          (ER)-derived protein bodies. The accumulation of zein
          in these ER-derived protein bodies results in the
          formation of the endosperm - the food storage body of
          seeds.
          Currently, there are four classes of zein: α, β, γ, and δ.
          These classes are expressed sequentially in maize
          and are found to interact with each other for stability.
          Zein from corn was reported to be approximay
          35% α-zein, which includes 2 prominent bands of
          22 and 24 kDa. β-zein fails to enter an SDS-PAGE gel
          without reduction. Reducing SDS-PAGE analysis
          shows that β-zein has 3 major bands of 24, 22, and
          14 kDa.1 The amino acid sequences have been
          published.2

           

          Precautions and Disclaimer
          For Laboratory Use Only. Not for drug, household or
          other uses.
          Preparation Instructions
          Zein is soluble in aqueous alcohols, glycols, ethyl
          ether, furfuryl alcohol, tetrahydrofurfuryl alcohol, and
          aqueous alkaline solutions of pH 11.5 or greater. Zein
          is insoluble in water, acetone, and anhydrous alcohols
          (except methanol).
          Storage/Stability
          Zein is rapidly denatured in solution and becomes
          insoluble.
          References
          1. Esen, A., Separation of alcohol-soluble proteins
          (zeins) from maize into three fractions by
          differential solubility. Plant Physiol., 80, 623-627
          (1986).
          2. Phillips, R. L., and McClure, B. A., Elevated
          protein-bound methionine in seeds of a maize line
          resistant to lysine plus threonine. Cereal Chem.,
          62, 213-218 (1985).

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