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Human milk ribonuclease

B K Dalaly, R R Eitenmiller, B A Friend

    Biochimica Et Biophysica Acta
    |October 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    Two ribonuclease (RNAase) components were isolated from human milk. These enzymes effectively degrade RNA, with optimal activity at pH 7.7 and 60°C, and show similarities to bovine pancreatic RNAase.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Milk Composition

    Background:

    • Human milk contains various bioactive components.
    • Ribonucleases (RNAases) are enzymes that degrade RNA.
    • Understanding milk enzymes is crucial for infant nutrition and health.

    Purpose of the Study:

    • To isolate and characterize ribonuclease (RNAase) components from human milk.
    • To determine the enzymatic properties and substrate specificity of human milk RNAase.
    • To compare human milk RNAase with other known RNAases.

    Main Methods:

    • Isolation of two RNAase components using polyacrylamide gel electrophoresis and ultracentrifugation.
    • Characterization of the major component's molecular weight, isoelectric point, and absorbance spectrum.

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  • Enzymatic assays to determine substrate specificity, optimal pH, and temperature.
  • Amino acid analysis and tryptic hydrolysis for structural comparison.

    • Main Results:

    • Two distinct human milk RNAase components were identified.
    • The major component has a molecular weight of ~14,000 Da, pI of 7.9, and hydrolyzes yeast RNA, poly(C), and poly(U).
    • Optimal activity is at pH 7.7 and 60°C; activity is modulated by various salts and divalent cations.

    Conclusions:

    • Human milk contains active ribonuclease enzymes with specific substrate preferences.
    • The characterized human milk RNAase shares some structural similarities with bovine pancreatic RNAase.
    • These findings contribute to the understanding of enzymatic activities in human milk.