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A complete cDNA coding for the sequence of glycinin A 2 B 1a subunit precursor
Author(s) -
Momma Takayuki,
Negoro Takaharu,
Udaka Kyoko,
Fukazawa Chikafusa
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)80886-3
Subject(s) - legumin , protein subunit , complementary dna , homology (biology) , amino acid , storage protein , peptide sequence , signal peptide , biochemistry , biology , protein primary structure , gene , scn3a , microbiology and biotechnology , chemistry , g alpha subunit
Analysis of the A 2 B 1a subunit precursor, one of the A 2 ‐subunit family of glycinin, the main storage protein of soybean, revealed that it is composed of a signal peptide segment (18 amino acids), the A 2 acidic polypeptide (282 amino acids), followed by the B 1a basic polypeptide (185 amino acids). There was overall 63% homology between this subunit complex and pea legumin, which is an analogous protein to glycinin. As this degree of homology is rather higher than that in the A 3 B 4 subunit, one of the A 3 subunit family, it seems that the genes encoding the A 2 subunit family are phylogenetically more strongly related to the legumin genes.