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Complete amino acid sequence of the A chain of mistletoe lectin I
M Huguet Soler1, S Stoeva, C Schwamborn
1Abteilung für Physikalische Biochemie des Physiologisch-chemischen Instituts der Universität Tübingen, Germany.
Abstract:
The complete amino acid sequence of the A chain of mistletoe lectin I was determined via Edman degradation sequencing of the N-terminus and tryptic and endoproteinase Asp-N overlapping fragments, amino acid analysis and MALDI-MS. The data obtained show a great homology with the chains of ribosome-inactivating proteins such as ricin and abrin with 111 (abrin-a) and 103 (ricin-D) amino acid residues conserved, respectively. The knowledge of the primary structure of MLA will have a fundamental impact on elucidating the biological function of medically applied mistletoe lectins on a molecular basis.