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

William D. Park | Zendy; Cheri Blackwood | Zendy; Greg A. Mignery | Zendy; Mark A. Hermodson | Zendy; Richard M. Lister | Zendy

Open Access

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

Author(s) -

William D. Park,

Cheri Blackwood,

Greg A. Mignery,

Mark A. Hermodson,

Richard M. Lister

Publication year - 1983

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.71.1.156

Subject(s) - solanum tuberosum , glycoprotein , polyacrylamide gel electrophoresis , immunodiffusion , biochemistry , molecular mass , gel electrophoresis , chemistry , immunoelectrophoresis , homology (biology) , sodium dodecyl sulfate , amino acid , peptide sequence , ouchterlony double immunodiffusion , electrophoresis , cultivar , biology , chromatography , genetics , botany , gene , antibody , enzyme , antiserum

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 NH(2)-terminal amino acid sequence analysis.

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