Complete Amino Acid Sequence of 14 kDa -Galactoside-Binding Lectin of Chick Embryo

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Abstract
The complete amino acid sequence of a soluble β-galactoside-binding lectin (subunit MW 14,500) of chick embryo was determined. The protein consists of 134 amino acids beginning with serine and ending with glutamic acid, and its N-terminal was blocked with acetate. The agreement of the present result with that obtained from nucleotide sequence analysis (Y. Ohyama et al. (1986) Biochem. Biophys. Res. Commun. 134, 51–56) indicates the lack of a cleavable leader sequence. Internal homologies were observed in several regions along the polypeptide chain. The highest homology (55% identity) was found between residues 42–58 and residues 112–128. This suggests that chick 14 kDa lectin may have evolved via several gene duplications.