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[Multiple forms of horse pepsin].

M V Gonchar, G I Lavrenova, G N Rudenskaia

    Biokhimiia (Moscow, Russia)
    |June 1, 1984
    PubMed
    Summary
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    Researchers isolated eight pepsin forms from horse gastric juice, revealing structural similarities and minor functional differences. These horse pepsin isoenzymes likely evolved recently from a common gene, showing early divergence.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Pepsin is a key digestive enzyme in mammals.
    • Multiple forms (isoenzymes) of pepsin exist, suggesting complex regulation and function.
    • Understanding pepsin diversity aids in comprehending digestive processes and evolutionary relationships.

    Purpose of the Study:

    • To isolate and characterize multiple pepsin forms from horse gastric juice.
    • To investigate the structural and functional relationships among these pepsin isoenzymes.
    • To explore the evolutionary origins of horse pepsin diversity.

    Main Methods:

    • Ion-exchange chromatography
    • Affinity chromatography
    • Isoelectric focusing (isoelectrofocusing)

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  • Molecular weight determination
  • Amino acid composition analysis
  • N-terminal sequencing
  • Tryptic peptide analysis

    • Main Results:

    • Eight distinct pepsin forms with isoelectric points (pI) ranging from 1.6 to 3.6 were isolated.
    • Identical structures were found among pepsin forms with pI 1.8, 2.1, 2.3, and 2.6, differing from the pI 3.2 form by four amino acid substitutions.
    • All isolated horse pepsin forms exhibited very similar functional activities.
    • The studied pepsin forms are evolutionarily related to pepsin A, more so than to other mammalian gastric aspartyl proteinases like gastricsin or chymosin.

    Conclusions:

    • Horse gastric juice contains a diverse set of pepsin isoenzymes.
    • These isoenzymes likely arose from recent gene duplication events, indicating early stages of structural and functional divergence.
    • The findings suggest a closer evolutionary relationship of these horse pepsins to pepsin A.