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Rat renin: purification and characterization

T Matoba, K Murakami, T Inagami

    Biochimica Et Biophysica Acta
    |October 12, 1978
    PubMed
    Summary
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    Rat kidney renin was purified into three isoenzymes (R-I, R-II, R-III) with similar amino acid compositions but differing molecular weights and isoelectric points. These rat renin isoenzymes exhibit high specific activity and a preference for rat substrates.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Renin (EC 3.4.99.19) is a key enzyme in the renin-angiotensin system, regulating blood pressure.
    • Understanding rat renin's unique molecular properties is crucial for hypertension research in rats.

    Purpose of the Study:

    • To purify rat kidney renin and characterize its isoenzymes.
    • To provide foundational data for high blood pressure studies utilizing rat models.

    Main Methods:

    • Renin purification from rat kidney using CM-cellulose chromatography.
    • Homogeneity assessment by multiple criteria.
    • Amino acid composition analysis.
    • Glycoprotein characterization using concanavalin A.
    • Molecular weight determination via SDS-PAGE.

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  • Isoelectric point determination.
  • Specific activity assays using rat plasma and synthetic peptide substrates.

    • Main Results:

    • Rat renin was separated into three major isoenzymes (R-I, R-II, R-III) with distinct molecular weights (37,000, 36,000, 35,000 Da) and isoelectric points (5.05, 5.15, 5.22).
    • Isoenzymes shared similar amino acid compositions, analogous to hog renin but with higher cysteine content.
    • Rat renin lacks amino sugars but is a glycoprotein; it shows high specific activity (615-626 Goldblatt units/mg) and prefers rat-derived substrates.
    • Active site analysis revealed similarities to hog renin, indicated by comparable catalytic rate constants with synthetic substrates.

    Conclusions:

    • Rat kidney renin exists as multiple isoenzymes with distinct physicochemical properties.
    • Rat renin exhibits unique glycosylation patterns and substrate specificity compared to hog renin.
    • The purified rat renin isoenzymes serve as valuable tools for studying the renin-angiotensin system and hypertension in rat models.