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Related Experiment Videos

Renin: structural features of active enzyme and inactive precursor.

T Inagami, J J Chang, C W Dykes

    Federation Proceedings
    |July 1, 1983
    PubMed
    Summary

    Researchers elucidated renin

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protease research

    Background:

    • Renin's catalytic mechanism and inactive form activation remain incompletely understood.
    • Acid proteases share structural similarities, but renin's unique aspects require detailed investigation.

    Purpose of the Study:

    • To elucidate the structural basis of renin's unique catalytic mechanism.
    • To determine the activation mechanism of inactive renin.

    Main Methods:

    • Isolation of pure active and inactive renin from various sources (human plasma, kidney; mouse submaxillary gland; hog kidney).
    • Determination of the complete amino acid sequence of mouse submaxillary gland renin.
    • Comparative sequence analysis with porcine pepsin.
    • Chromatographic separation techniques.
    • Investigation of inactive renin activation using proteolysis and dissociative reagents.

    Main Results:

    • The active site of renin contains two aspartyl, two tyrosyl, and one arginyl residue, similar to pepsin.
    • Mouse submaxillary gland renin shares 43% amino acid identity with porcine pepsin.
    • Inactive renin was purified and found to be a single polypeptide chain.
    • Inactive renin activation is mediated by proteolysis, not by dissociative agents like 4 M NaCl or detergents.

    Conclusions:

    • Inactive renin in the studied tissues represents a renin zymogen.
    • The findings provide insights into renin's catalytic function and activation pathways.

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