Enzymes: alkaline phosphatase (EC 3.1.3.1); lysylendopeptidase (EC 3.4.21.50); restriction endonucleases EcoRI (EC 3.1.21.4) and NcoI (EC 3.1.31.4); thioredoxin reductase (EC 1.8.1.9); tyrosine kinase (EC 2.7.1.112).
Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein
Article first published online: 21 MAY 2003
DOI: 10.1046/j.1432-1033.2003.03627.x
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How to Cite
Hanada, K., Nishiuchi, Y. and Hirano, H. (2003), Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein. European Journal of Biochemistry, 270: 2583–2592. doi: 10.1046/j.1432-1033.2003.03627.x
Note: As the binding capabilities of insulin and the 4-kDa peptide to the 43 kDa protein were similar, Watanabe et al. named the 4-kDa peptide as leginsulin in their early publication. There are many controversies related to the naming of this peptide as leginsulin. To avoid confusion, in the present article we referred to the peptide as ‘4-kDa peptide’ instead of leginsulin.
Publication History
- Issue published online: 21 MAY 2003
- Article first published online: 21 MAY 2003
- (Received 28 February 2003, revised 16 April 2003, accepted 22 April 2003)
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