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Related Experiment Videos

[Beta-cyanoalanine synthase: Its purification and basic physico-chemical properties].

T N Akopian, E V Goriachenkova

    Biokhimiia (Moscow, Russia)
    |May 1, 1976
    PubMed
    Summary

    Researchers purified beta-cyano-L-alanine synthase from blue lupine seedlings. This enzyme, crucial for amino acid synthesis, was isolated with high purity and characterized, yielding valuable data on its properties.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Plant Science

    Context:

    • Beta-cyano-L-alanine synthase is a key enzyme in amino acid metabolism.
    • Purification of this enzyme from plant sources is essential for detailed biochemical studies.
    • Etiolated blue lupine seedlings provide a source for enzyme isolation.

    Purpose:

    • To develop a method for purifying beta-cyano-L-alanine synthase.
    • To characterize the physical and chemical properties of the purified enzyme.
    • To investigate the enzyme's cofactor requirements and spectral characteristics.

    Summary:

    • A purification protocol for beta-cyano-L-alanine synthase from blue lupine seedlings yielded preparations with over 4000-fold specific activity.
    • Electrophoresis confirmed enzyme homogeneity, with a molecular weight of 52000 and glutamic acid as the N-terminal amino acid.

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  • The enzyme contains one mole of pyridoxal-P per mole of protein, exhibiting a characteristic absorption maximum at 410 nm.

    • Impact:

    • Provides highly purified beta-cyano-L-alanine synthase for further functional and structural analysis.
    • Contributes to understanding pyridoxal-phosphate-dependent enzymes in plants.
    • Offers insights into amino acid biosynthesis pathways in legumes.