Complete amino acid sequence of the A chain of mistletoe lectin I.
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.
Huguet Soler
M
M
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Instituts der Universität Tübingen, Germany.
Stoeva
S
S
Schwamborn
C
C
Wilhelm
S
S
Stiefel
T
T
Voelter
W
W
D000595:Amino Acid Sequence; D037102:Lectins / Q000737:chemistry*; D014784:Mistletoe / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D010946:Plants, Medicinal; D054790:Ribosome Inactivating Proteins, Type 2; D017386:Sequence Homology, Amino Acid; D014118:Toxins, Biological / Q000737:chemistry*
D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; C009674:ribosome inactivating protein, Viscum