Laburnum

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Toshiaki Osawa - One of the best experts on this subject based on the ideXlab platform.

  • Correlation between carbohydrate‐binding specificity and amino acid sequence of carbohydrate‐binding regions of Cytisus‐type anti‐H(O) lectins
    FEBS Letters, 1992
    Co-Authors: Yukiko Konami, Kazuo Yamamoto, Toshiaki Osawa, Tatsuro Irimura
    Abstract:

    A carbohydrate-binding peptide of the di-N-acetylchitoblose-binding Cytisus sessilifolius anti-H(O) lectin I (CSA-I) was isolated from the endoproteinase Asp-N digest of CSA-I by affinity chromatography on a column of N-acetyl-d-glucosamine oligomer-Sepharose (GIcNAc oligomer-Sepharose). The amino acid sequence of the carbohydrate-binding peptide of CSA-I was determined to be DTYFGKTYNPW using a gas-phase protein sequencer. This sequence corresponds to the sequence from Asp-129 to Trp-139 based on the primary structure of CSA-I, and shows a high degree of homology to those of the putative carbohydrate-binding peptide of the Laburnum alpinum lectin I (LAA-I) (DTYFGKAYNPW) and of the Ulex europaeus lectin II (UEA-II) (DSYFGKTYNPW). The binding of these three anti-H(O) lectins is known to be inhibited by di-N-acetylchitobiose but not by l-fucose. These results strongly suggest that there is a good correlation between the carbohydrate-binding specificity and the amino acid sequence of the carbohydrate-binding regions of di-N-acetylchitobiose-binding lectins.

  • Carbohydrate-binding peptides from several anti-H(O) lectins.
    Journal of Biochemistry, 1992
    Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro Irimura
    Abstract:

    Peptide fragments have been obtained from L-fucose-binding anti-H(O) lectins [Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I)] and di-N-acetylchitobiose-binding anti-H(O) lectins [Ulex europeus lectin II (UEA-II) and Laburnum alpinum lectin I (LAA-I)] by treatment with endoproteinase Asp-N or Lys-C. The peptide fragments were fractionated by affinity chromatography on a column of Fuc-Gel for LTA and UEA-I, and on a column of N-acetyl-D-glucosamine oligomer-Sepharose for UEA-II and LAA-I. The peptides with affinity for these columns were identified by peptide sequencing. All of these retarded peptides were found to be parts of the metal-binding regions of these lectins. It is strongly suggested that these peptides represent the carbohydrate-binding and metal ion-binding sites of legume lectins, respectively.

  • the primary structure of the Laburnum alpinum seed lectin
    FEBS Letters, 1991
    Co-Authors: Yukiko Konami, Kazuo Yamamoto, Satoshi Toyoshima, Toshiaki Osawa
    Abstract:

    The complete amino acid sequence of the Laburnum alpinum di-N-acetylchitobiose-binding lectin was determined by using a protein sequencer after digestion with endoproteinases Lys-C and Asp-N, and compared with those of other leguminous plant lectins.

F C Czygan - One of the best experts on this subject based on the ideXlab platform.

  • uber die alkaloidzusammensetzung der oberirdischen teile von Laburnum watereri kirchn dipp
    Biochemie und Physiologie der Pflanzen, 1990
    Co-Authors: Roland Greinwald, Wulf Schultze, F C Czygan
    Abstract:

    Summary The alkaloid composition of the overground parts (leaves, petioles, stems, flowers, fruits and seeds) of Laburnum watereri (hybrid of Laburnum alpinum × L. anagyroides ) and its seasonal changes (from march to november) have been studied by different chromatographic (TLC, capillary GC) and spectroscopic (GC/MS, HRMS, 1 H-NMR, 13 C-NMR, IR, UV) methods. Seeds only contain cytisine. Besides cytisine, traces of methylcytisine and ammodendrine 12 further alkaloids could be identified in the fruits, among which β-isosparteine, 14e-hydroxysparteine and epi-baptifoline have been found for the first time in the genus Laburnum . Following the seasonal changes of the alkaloid composition of the fruits, an increase of epibaptifoline and ammodendrine was established during ripening, while the content of the main compound cytisine strongly declined. The highest total amount of alkaloids (with 80 to 90% cytisine) was found in the buds in the spring. During the further development of the leaves, the cystine content decreases and a methylation of this alkaloid begins. In summer the alkaloid concentration reaches the lowest level. In the course of July epi-baptifoline (erroneously reported as methylcytisine in literature) increases and becomes the main alkaloid for the following 6 months.

  • cytisine 12 carboxy ethylester a quinolizidine alkaloid from Laburnum watereri and its occurrence in the leguminosae
    Phytochemistry, 1990
    Co-Authors: R Greinwald, Peter Bachmann, Ludger Witte, F C Czygan
    Abstract:

    Abstract A new lupin alkaloid, cytisine-12-carboxy-ethylester, was isolated from suspension cultures of Laburnum watereri. Its structure was determined by spectroscopic data and by direct comparison with a synthetic sample. The distribution of the new alkaloid amongst different genera of the Leguminosae is reported.

Yukiko Konami - One of the best experts on this subject based on the ideXlab platform.

  • Correlation between carbohydrate‐binding specificity and amino acid sequence of carbohydrate‐binding regions of Cytisus‐type anti‐H(O) lectins
    FEBS Letters, 1992
    Co-Authors: Yukiko Konami, Kazuo Yamamoto, Toshiaki Osawa, Tatsuro Irimura
    Abstract:

    A carbohydrate-binding peptide of the di-N-acetylchitoblose-binding Cytisus sessilifolius anti-H(O) lectin I (CSA-I) was isolated from the endoproteinase Asp-N digest of CSA-I by affinity chromatography on a column of N-acetyl-d-glucosamine oligomer-Sepharose (GIcNAc oligomer-Sepharose). The amino acid sequence of the carbohydrate-binding peptide of CSA-I was determined to be DTYFGKTYNPW using a gas-phase protein sequencer. This sequence corresponds to the sequence from Asp-129 to Trp-139 based on the primary structure of CSA-I, and shows a high degree of homology to those of the putative carbohydrate-binding peptide of the Laburnum alpinum lectin I (LAA-I) (DTYFGKAYNPW) and of the Ulex europaeus lectin II (UEA-II) (DSYFGKTYNPW). The binding of these three anti-H(O) lectins is known to be inhibited by di-N-acetylchitobiose but not by l-fucose. These results strongly suggest that there is a good correlation between the carbohydrate-binding specificity and the amino acid sequence of the carbohydrate-binding regions of di-N-acetylchitobiose-binding lectins.

  • Carbohydrate-binding peptides from several anti-H(O) lectins.
    Journal of Biochemistry, 1992
    Co-Authors: Kazuo Yamamoto, Yukiko Konami, Toshiaki Osawa, Tatsuro Irimura
    Abstract:

    Peptide fragments have been obtained from L-fucose-binding anti-H(O) lectins [Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I)] and di-N-acetylchitobiose-binding anti-H(O) lectins [Ulex europeus lectin II (UEA-II) and Laburnum alpinum lectin I (LAA-I)] by treatment with endoproteinase Asp-N or Lys-C. The peptide fragments were fractionated by affinity chromatography on a column of Fuc-Gel for LTA and UEA-I, and on a column of N-acetyl-D-glucosamine oligomer-Sepharose for UEA-II and LAA-I. The peptides with affinity for these columns were identified by peptide sequencing. All of these retarded peptides were found to be parts of the metal-binding regions of these lectins. It is strongly suggested that these peptides represent the carbohydrate-binding and metal ion-binding sites of legume lectins, respectively.

  • the primary structure of the Laburnum alpinum seed lectin
    FEBS Letters, 1991
    Co-Authors: Yukiko Konami, Kazuo Yamamoto, Satoshi Toyoshima, Toshiaki Osawa
    Abstract:

    The complete amino acid sequence of the Laburnum alpinum di-N-acetylchitobiose-binding lectin was determined by using a protein sequencer after digestion with endoproteinases Lys-C and Asp-N, and compared with those of other leguminous plant lectins.

K Becker - One of the best experts on this subject based on the ideXlab platform.

R Greinwald - One of the best experts on this subject based on the ideXlab platform.