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Analysis of the Heterogeneity of the 40,000 Molecular Weight Tuber Glycoprotein of Potatoes by Immunological Methods and by NH₂-Terminal Sequence Analysis ¹

Department of Horticulture, Purdue University, West Lafayette, Indiana 47907, Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907

Among the major soluble tuber proteins of potato (Solanum tuberosum L.) is a group of glycoproteins having apparent molecular weights of approximately 40,000. This group of proteins as purified by ion-exchange and affinity chromatography has been given the trivial name `patatin.' Patatin exists in a number of charge forms which differ between potato cultivars and in some cases can also be resolved into a number of bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, by immunodiffusion and immunoelectrophoresis, it was found that the isoforms of patatin are immunologically identical both within a cultivar as well as between cultivars. A high degree of homology between the isoforms of patatin is also indicated by NH₂-terminal amino acid sequence analysis.

¹ Supported by funds from the Purdue University Agricultural Experiment Station and by Grant 59-2182-1-1-615-0 from the United States Department of Agriculture. Journal Paper 8949 of the Purdue University Agricultural Experiment Station.

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