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J. Biol. Chem., Vol. 265, Issue 35, 21573-21579, Dec, 1990
Y Sakakura, J Hirabayashi, Y Oda, Y Ohyama and K Kasai
The complete primary structure of chicken 16-kDa beta-galactoside- binding
lectin (C-16) was determined. It was composed of 134 amino acid residues
and has an acetylated NH2 terminus. A cDNA was also cloned, but no signal
sequence was found in the initiator region. The initiator methionine
remained as the NH2 terminus of the mature lectin. Although C-16 is
distinct from chicken 14-kDa beta-galactoside-binding lectin (C- 14), it
proved to be a member of the vertebrate 14-kDa-type lectin family.
Comparison of the primary structures between the vertebrate 14- kDa-type
lectins suggests that C-14 and C-16 were produced by gene duplication of an
ancestral lectin gene at a time close to the divergence of birds and
mammals. Northern and Southern blot analysis indicated that these
isolectins are encoded by individual genes which are differently regulated
during the development of the embryo. A recombinant C-16 lectin was
produced in Escherichia coli. The product was indistinguishable from the
authentic C-16 lectin except that the NH2 terminus of the former was found
to begin with free methionine.
Structure of chicken 16-kDa beta-galactoside-binding lectin. Complete amino acid sequence, cloning of cDNA, and production of recombinant lectin
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
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