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Complete Amino Acid Sequence of Soybean Leaf P21
Author(s) -
John S. Graham,
William Burkhart,
Jin Xiong,
Jeffrey W. Gillikin
Publication year - 1992
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.98.1.163
Subject(s) - thaumatin , glycine , isoelectric point , amino acid , peptide sequence , biology , isoelectric focusing , biochemistry , wine tasting , chemistry , gene , food science , wine , enzyme
A polypeptide structurally related to the thaumatin family of proteins has been purified from soybean (Glycine max) leaves and the complete amino acid sequence has been determined. The mature protein, which we have termed P21, has a calculated molecular weight of 21,461 and an isoelectric point of 4.6. The soybean protein shows 64% amino acid identity with thaumatin, a sweet-tasting protein found in the West African shrub Thaumatococcus danielli, and as much as 71% identity with thaumatin-like polypeptides present in tobacco and maize.

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