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Identification of Tall Fescue Cultivars by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis of Seed Proteins
Author(s) -
Krishnan Hari B.,
Sleper David A.
Publication year - 1997
Publication title -
crop science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.76
H-Index - 147
eISSN - 1435-0653
pISSN - 0011-183X
DOI - 10.2135/cropsci1997.0011183x003700010037x
Subject(s) - cultivar , biology , polyacrylamide gel electrophoresis , globulin , sodium dodecyl sulfate , gel electrophoresis , agronomy , festuca arundinacea , poaceae , botany , biochemistry , immunology , enzyme
Tall fescue ( Festuca arundinaceae Schreb.) is a cool‐season grass used widely for turf and forage. There is a steady increase in the number of new cultivars of tall fescue that are released through the effort of plant breeders. Most of these cultivars are closely related in pedigree and are similar phenotypically. As a result, identification of tall fescue cultivars has become increasingly cumbersome. The purpose of this study was to develop an electrophoretic procedure which will aid in routine identification of different cultivars of tall fescue. We isolated salt‐soluble globulins and alcohol‐soluble prolamines from nine tall fescue cultivars and resolved them by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE). Salt soluble globulins were very similar in their polypeptide profiles and hence offered little promise in cultivar identification. However, SDS‐PAGE analysis of seed prolamines effectively differentiated the tall fescue cultivars on the basis of presence and absence of unique polypeptides. Subtle differences in the banding patterns of prolamines of closely related cultivars were enhanced by computer assisted densitometer scans. The results of this study indicate that SDS‐PAGE analysis of alcohol‐soluble prolamines can be used as a rapid and reliable method for identification of tall fescue cultivars.