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Post-proline cleaving enzyme from lamb brain

T Yoshimoto, W H Simmons, T Kita

    Journal of Biochemistry
    |August 1, 1981
    PubMed
    Summary
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    This study purified a post-proline cleaving enzyme from lamb brain, detailing its substrate specificity and structural properties. The enzyme

    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Post-proline cleaving enzyme (PPCE) plays a role in neuropeptide metabolism.
    • Understanding PPCE is crucial for elucidating its physiological functions.

    Purpose of the Study:

    • To purify and characterize post-proline cleaving enzyme from lamb brain.
    • To compare its properties with the lamb kidney enzyme.

    Main Methods:

    • Purification using DEAE-Sephadex, hydroxyapatite, and Sephadex G-150 chromatography.
    • Enzyme activity assays with various peptide substrates.
    • Substrate specificity analysis and subsite mapping.
    • Molecular weight determination via gel filtration and SDS-PAGE.
    • Isoelectric point determination.

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    Main Results:

    • Homogeneous PPCE was purified from lamb brain.
    • The enzyme hydrolyzed various peptide hormones at proline residues.
    • Subsite mapping revealed five subsites (S3 to S2') with high stereospecificity.
    • Molecular weight was estimated to be 74,000-77,000 Da.
    • Enzyme activity was inhibited by DFP, PCMB, Hg2+, and Cu2+.

    Conclusions:

    • Lamb brain PPCE shares properties with the lamb kidney enzyme.
    • The study refined the molecular weight of the lamb kidney PPCE to 74,000 Da.
    • These findings contribute to the understanding of proline-specific endopeptidases.