Botanisches Institut der Universität, Meckenheimer Allee 170, D-5300, Bonn 1, Federal Republic of Germany.
Planta. 1986 Sep;168(3):386-9. doi: 10.1007/BF00392365.
Antibodies were raised against the highly purified glycoprotein patatin. They were used to characterize the product synthesized in a wheatgerm cell-free translation system, programmed with polyadenylated RNA from potato tubers. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed that the immunoprecipitated protein had a molecular mass of 43 kDa compared to 40 for the authentic patatin. It is assumed that patatin is synthesized in vivo as a larger precursor which is processed to the mature protein by cleavage of a signal peptide. Our results are in agreement with sequence-analysis data of patatin complementary DNA which indicate a signal peptide of about 23 amino acids (Mignery et al., 1984; Nucleic Acids Res. 12, 7987-8000).
针对高度纯化的马铃薯油蛋白制备了抗体。利用这些抗体对从小麦胚芽无细胞翻译系统中转录多聚腺苷酸化 RNA 合成的产物进行了鉴定，该系统中转录的模板来自于马铃薯块茎。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示，免疫沉淀的蛋白分子量为 43kDa，而天然马铃薯油蛋白分子量为 40kDa。推测马铃薯油蛋白在体内合成时为较大的前体，通过信号肽的切割加工成成熟蛋白。我们的结果与马铃薯油蛋白 cDNA 的序列分析数据一致，该数据表明信号肽约有 23 个氨基酸（Mignery 等人，1984 年；核酸研究 12，7987-8000）。
