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Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins
- Source :
- Phytochemistry. 64:701-708
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- Soybean (Glycine max L.) storage proteins are composed mainly of two major components, beta-conglycinin and glycinin. Electrophoretic variants of the beta subunit of beta-conglycinin and the A3 polypeptide of glycinin were detected on SDS-PAGE, and designated them as beta* and A3*, respectively. beta* and A3* exhibited higher and lower mobilities, respectively, than the common beta subunit and A3 polypeptide. The N-terminal nine and 10 amino acid sequences of beta* and A3* were completely identical to the previously reported sequences of the beta subunit and the A3 polypeptide, respectively. Analysis using concanavalin A-horseradish peroxidase and treatment with N-glycosidase indicated that glycans were not responsible for the difference in electrophoretic mobility of beta* or A3*. Furthermore, five clones of beta* or beta and three clones of A3*, respectively, were sequenced but we could not detect deletions and insertions except for a single or a few amino acid substitutions as compared with the common beta subunit and A3 polypeptide. These results indicate that a single or a few amino acid substitution affects the electrophoretic mobilities of beta* and A3*.
- Subjects :
- Glycan
Hot Temperature
Glycoside Hydrolases
Molecular Sequence Data
Plant Science
Horticulture
Biochemistry
Drug Stability
Concanavalin A
Protein Isoforms
Storage protein
Amino Acid Sequence
Cloning, Molecular
Molecular Biology
Horseradish Peroxidase
Glycoproteins
chemistry.chemical_classification
Calorimetry, Differential Scanning
Sequence Homology, Amino Acid
biology
Seed Storage Proteins
Globulins
Amino acid substitution
General Medicine
Antigens, Plant
Molecular biology
Amino acid
Protein Subunits
Electrophoresis
chemistry
Seeds
Glycine
Soybean Proteins
biology.protein
Electrophoresis, Polyacrylamide Gel
Soybeans
Sequence Alignment
Peroxidase
Subjects
Details
- ISSN :
- 00319422
- Volume :
- 64
- Database :
- OpenAIRE
- Journal :
- Phytochemistry
- Accession number :
- edsair.doi.dedup.....822679d812fc00a05d56e8c3d4813348