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Characterization of human angiotensinogen.

D A Tewksbury, W L Frome, M L Dumas

    The Journal of Biological Chemistry
    |June 10, 1978
    PubMed
    Summary

    This study characterized human angiotensinogen, a glycoprotein. Researchers determined its molecular weight, amino acid sequence, and carbohydrate content, revealing anomalous behavior in electrophoresis.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Proteomics

    Background:

    • Human angiotensinogen is a key precursor in the renin-angiotensin system.
    • Understanding its physical and chemical properties is crucial for studying blood pressure regulation.

    Purpose of the Study:

    • To determine the physical and chemical properties of human angiotensinogen.
    • To investigate its behavior in sodium dodecyl sulfate electrophoresis.
    • To characterize its amino acid termini and carbohydrate content.

    Main Methods:

    • Sedimentation equilibrium studies for molecular weight determination.
    • Sodium dodecyl sulfate (SDS) electrophoresis and Ferguson-type plots.
    • Analysis of COOH-terminal and NH2-terminal amino acids.

    Main Results:

    • Human angiotensinogen is a glycoprotein with 14% carbohydrate and a molecular weight of 56,800.
    • It exhibits anomalous behavior on SDS electrophoresis, suggesting a higher molecular weight.
    • Serine was identified as the COOH-terminal amino acid, with alanine and aspartic acid/asparagine at the NH2-terminus.

    Conclusions:

    • Human angiotensinogen possesses distinct physical and chemical characteristics, including anomalous SDS-PAGE behavior.
    • Variations in angiotensin I content do not affect protein homogeneity.
    • A protein variant with negligible angiotensin I content was isolated, retaining serine at the COOH-terminus and alanine at the NH2-terminus.

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