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Complete amino acid sequence of the A chain of mistletoe lectin I. 1996

M Huguet Soler, and S Stoeva, and C Schwamborn, and S Wilhelm, and T Stiefel, and W Voelter
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Instituts der Universität Tübingen, Germany.

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.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D010946 Plants, Medicinal Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals. Herbs, Medicinal,Medicinal Herbs,Healing Plants,Medicinal Plants,Pharmaceutical Plants,Healing Plant,Herb, Medicinal,Medicinal Herb,Medicinal Plant,Pharmaceutical Plant,Plant, Healing,Plant, Medicinal,Plant, Pharmaceutical,Plants, Healing,Plants, Pharmaceutical
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D014118 Toxins, Biological Specific, characterizable, poisonous chemicals, often PROTEINS, with specific biological properties, including immunogenicity, produced by microbes, higher plants (PLANTS, TOXIC), or ANIMALS. Biological Toxins
D014784 Mistletoe Parasitic plants that form a bushy growth on branches of host trees which are in the order Santalales. It includes the Christmas mistletoe family (VISCACEAE), the showy mistletoe family (LORANTHACEAE) and the catkin mistletoe family (Eremolepidaceae). The composition of toxins, lectins, tyramine, phenethylamines, and other compounds may be affected by the host. Mistletoes
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D054790 Ribosome Inactivating Proteins, Type 2 Ribosome inactivating proteins consisting of two polypeptide chains, the toxic A subunit and a lectin B subunit, linked by disulfide bridges. The lectin portion binds to cell surfaces and facilitates transport into the ENDOPLASMIC RETICULUM.
D028321 Plant Preparations Material prepared from plants. Herbal Preparations,Herbal Preparation,Plant Preparation,Preparation, Plant

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