Analysis of the heterogeneity of the 40,000 molecular weight tuber glycoprotein of potatoes by immunological methods and by NH2-terminal sequence analysis

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 e...

Full description

Saved in:
Bibliographic Details
Published inPlant physiology (Bethesda) Vol. 71; no. 1; pp. 156 - 160
Main Authors Park, W.D, Blackwood, C, Mignery, G.A, Hermodson, M.A, Lister, R.M
Format Journal Article
LanguageEnglish
Published American Society of Plant Physiologists 1983
Subjects
Amino acids
Antibodies
Electrophoresis
Gels
Glycoproteins
Immunology
Potatoes
Protein isoforms
Sodium
Solanum tuberosum
Tubers
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:F60
8255295
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.71.1.156