Abstract
The complete amino acid sequence of the major a subunit of the lectin from seeds of Dioclea grandiflora was determined. The sequence was deduced from analysis of peptides derived from the native α subunit by digestion with trypsin, chymotrypsin, the Staphylococcus aureus V8 protease, and pepsin; and from larger peptides produced by digestion of the citraconylated protein with trypsin. The α subunit consists of a single polypeptide chain of 237 amino acids which differs from the sequence of concanavalin in 53 positions. Significant levels of heterogeneity were observed in five positions in the sequence. Copyright © 1984, Wiley Blackwell. All rights reserved
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CITATION STYLE
RICHARDSON, M., CAMPOS, F. D. A. P., MOREIRA, R. A., AINOUZ, I. L., BEGBIE, R., WATT, W. B., & PUSZTAI, A. (1984). The complete amino acid sequence of the major α subunit of the lectin from the seeds of Dioclea grandiflora (Mart). European Journal of Biochemistry, 144(1), 101–111. https://doi.org/10.1111/j.1432-1033.1984.tb08436.x
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