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).
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- Poly(A)+ RNA:
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
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Krischner, B., Hahn, H. Patatin, a major soluble protein of the potato (Solanum tuberosum L.) tuber is synthesized as a larger precursor. Planta 168, 386–389 (1986). https://doi.org/10.1007/BF00392365
- Patatin (biosynthesis, precursor)
- Signal peptide