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Related Experiment Videos

Apolipoprotein B is a globular protein--morphological studies by electron microscopy.

D M Lee, D L Stiers, T Mok

    Biochemical and Biophysical Research Communications
    |April 14, 1987
    PubMed
    Summary

    Water-soluble apolipoprotein B, a key component of low-density lipoproteins, was isolated and characterized. Morphological studies revealed it as a globular protein, with its calculated molecular weight aligning with amino acid sequence data.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Apolipoprotein B (apoB) is a crucial protein component of lipoproteins, particularly low-density lipoproteins (LDL).
    • Understanding the structure of apoB is essential for elucidating its role in lipid transport and cardiovascular disease.

    Purpose of the Study:

    • To prepare water-soluble apolipoprotein B (apoB) from plasma.
    • To determine the morphology and molecular weight of apoB using advanced imaging techniques.

    Main Methods:

    • Isolation of low-density lipoproteins (LDL) from fresh plasma.
    • Non-oxidative delipidation and protein denaturation using guanidine hydrochloride.
    • Reduction and carboxymethylation of apoB.
    • Purification via dialysis against urea and ammonium acetate buffers.

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  • Morphological analysis using electron microscopy (negative staining and freeze fracture).

    • Main Results:

    • Apolipoprotein B was successfully prepared in a water-soluble form.
    • Electron microscopy revealed apoB as a globular protein with an average diameter of 11.48 ± 1.25 nm.
    • The molecular weight calculated from particle size was consistent with data derived from amino acid sequencing.

    Conclusions:

    • Apolipoprotein B exists as a globular structure in its isolated, delipidated form.
    • The structural data obtained supports the established molecular weight of apoB.
    • This study provides valuable insights into the physical characteristics of apolipoprotein B.