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The complete amino acid sequences of the β 1 ‐ and β 2 ‐subunits of the isolectins LoL1 and LoL11 from seeds of Lathyrus ochrus (L.) DC
Author(s) -
Yarwood A.,
Richardson M.,
Sousa-Cavada B.,
Rougé P.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80663-3
Subject(s) - lathyrus , trypsin , chymotrypsin , biochemistry , chemistry , amino acid , lectin , pepsin , protease , peptide sequence , homology (biology) , biology , enzyme , botany , gene
The complete amino acid sequences of the β 1 ‐ and β 2 ‐subunits of the isolectins (LoL1 and LoL11) from seeds of Lathyrus ochrus were determined by analysis of peptides derived from the proteins by digestion with trypsin, chymotrypsin, pepsin and the S. aureus V 8 protease, as well as fragments produced by cleavage with iodosobenzoic acid. Both β‐subunits consisted of singlepolypeptide chains of 181 amino acids, which differed from one another in only 3 positions. The homology of the Lathyrus ochrus isolectins with the other two‐chain lectins of the tribe Vicieae, and the single‐chain lectins of other tribes of the Leguminosae is discussed.