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The lysine and methionine rich basic subunit of buckwheat grain legumin: Some results of a structural study
Author(s) -
Rout M. K.,
Chrungoo N. K.
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900202033
Subject(s) - legumin , lysine , methionine , protein subunit , random coil , arginine , biochemistry , chemistry , storage protein , protein secondary structure , biology , amino acid , gene
10.1080/15216549900202033.abs The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% α‐helix, 36% β‐sheet, 12% β‐turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin‐type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.