Abstract: A peptide (35kD) was purified by gel filteration with sephadex LH20 and SDS-PAGE from storage proteins of wheat. The peptide is a material which can be used to form peptide vesicles after being sonicated in some aqueous solvent. The peptide vesicles can wrap various compounds of molecular weight ranging from 0.4 to 150 kD. The peptide vesicles which wrap the compounds can be kept in stable state for months at 4℃ or for days at room temperature. The vesicles can be changed into scale state by freeze drying and scale state can be changed into state of vesicles by rehydrating. That is to say, they have the characterization of D R F (dehydration rehydration vesicles). The peptide vesicles prepared from modified protein can wrap water-soluble compounds, but they can only wrap hydrophobic compounds if the protein is not modified. It shows that the hydrophobic region is located inside membrane of the peptide vesicles. The protein contains 16 hydrophobic amino acid residues and a N-terminal Phe.

Key words: storage proteins of wheat, peptide vesicles, hydrophobic region

摘要： 小麦(Triticum aestivum)贮存蛋白经过纯化获得其中35kD一种蛋白质。该蛋白质在一定浓度的有机溶剂系统中经过超声波处理或搅拌，可以制成囊泡，并能包裹分子量从0.4～150kD的不同化合物(染料及抗体)。这种肽泡具有良好的稳定性，经低温冷冻干燥后，可成鳞片状，加水后复溶仍然保持肽泡的稳定性。这种特性称为DRV(Dehydration Rehydration Vesicles)性质。该蛋白质经修饰制定肽泡能包裹水溶性化合物，如水溶性染料，或不经修饰可包裹脂溶性化合物。这种蛋白质是由16种疏水性氨基酸残基组成，其N-末端为苯丙氨酸。

关键词: 小麦贮存蛋白, 肽泡, 疏水特性