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A pepsinogen from rainbow trout.

S S Twining, P A Alexander, K Huibregtse

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1983
    PubMed
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    Rainbow trout pepsinogen (Ia) activates optimally at pH 2. Its cognate pepsin, active at pH 3, shows similar reactivity to mammalian enzymes despite operating at fish environmental temperatures.

    Area of Science:

    • Biochemistry
    • Comparative Physiology
    • Enzymology

    Background:

    • Pepsinogen and pepsin are key digestive enzymes.
    • Understanding fish digestive enzymes provides insights into comparative physiology.
    • Rainbow trout (Oncorhynchus mykiss) are a model species for aquaculture and ecotoxicology.

    Purpose of the Study:

    • To characterize the biochemical properties of rainbow trout pepsinogen (Ia) and its cognate pepsin.
    • To compare the enzymatic activity and stability of trout pepsin with mammalian counterparts.

    Main Methods:

    • Electrophoretic mobility was used to identify pepsinogen Ia.
    • Enzyme activation and proteolysis assays were performed at various pH levels.
    • Stability assays were conducted at different pH values.

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    Main Results:

    • Rainbow trout pepsinogen Ia optimally activates at pH 2.
    • The resulting pepsin exhibits optimal proteolysis at pH 3.
    • Trout pepsin is denatured above pH 7, while the zymogen shows slightly greater alkali stability.
    • The intrinsic reactivity of trout pepsinogen and pepsin is high, comparable to mammalian enzymes at physiological temperatures.

    Conclusions:

    • Rainbow trout pepsinogen and pepsin possess biochemical characteristics suitable for efficient digestion in their natural environment.
    • The comparable reactivity to mammalian enzymes suggests conserved functional properties in vertebrate pepsinogens.