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Related Experiment Videos

L-[1-11C]leucine: routine synthesis by enzymatic resolution.

J R Barrio, R E Keen, J R Ropchan

    Journal of Nuclear Medicine : Official Publication, Society of Nuclear Medicine
    |June 1, 1983
    PubMed
    Summary
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    A new method synthesizes L-[1-11C]leucine for brain protein synthesis studies. Immobilized enzymes efficiently resolve enantiomers, yielding a pure, sterile product for positron emission tomography (PET) scans.

    Area of Science:

    • Biochemistry
    • Radiochemistry
    • Neuroscience

    Background:

    • Cerebral protein synthesis is crucial for brain function.
    • Positron emission tomography (PET) requires radiolabeled tracers like L-[1-11C]leucine.
    • Accurate determination of protein synthesis rates necessitates enantiomerically pure tracers.

    Purpose of the Study:

    • To develop a synthesis method for enantiomerically pure L-[1-11C]leucine.
    • To enable precise measurement of cerebral protein synthesis rates using PET.
    • To ensure a high-purity, sterile radiotracer suitable for human studies.

    Main Methods:

    • Modified Bucherer-Strecker reaction for initial synthesis.
    • Immobilized D-amino acid oxidase/catalase enzyme complex on Sepharose for enantiomeric resolution.

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  • Semiautomated synthesis system for rapid production.

    • Main Results:

    • Achieved radiochemical purity greater than 99% for L-[1-11C]leucine.
    • Obtained a radiochemical yield of 25%.
    • Production time of 30-40 minutes after H11CN preparation.

    Conclusions:

    • The developed method provides a reliable and efficient synthesis of enantiomerically pure L-[1-11C]leucine.
    • Immobilized enzyme technology ensures a sterile, pyrogen-free product, suitable for PET imaging.
    • This tracer facilitates accurate assessment of cerebral protein synthesis in humans.