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Protein sequence analysis: automated microsequencing.

M W Hunkapiller, L E Hood

    Science (New York, N.Y.)
    |February 11, 1983
    PubMed
    Summary
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    Automated protein microsequencing is now possible at the submicrogram level using polypeptides from gel electrophoresis. This technique works for both small peptides and large proteins.

    Area of Science:

    • Biochemistry
    • Proteomics
    • Analytical Chemistry

    Background:

    • Protein identification and characterization are crucial in biological research.
    • Traditional protein sequencing methods often require larger sample amounts.
    • Advances in gel electrophoresis have enabled better isolation of protein samples.

    Purpose of the Study:

    • To present a highly sensitive automated microsequencing technique for proteins.
    • To demonstrate the applicability of the method to various polypeptide sizes.
    • To enable protein analysis from samples obtained directly from gel electrophoresis.

    Main Methods:

    • Automated protein microsequencing.
    • Sample preparation from one- and two-dimensional gel electrophoresis.

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  • Analysis of polypeptides ranging from small peptides to large proteins.

    • Main Results:

    • Successful protein microsequencing at the 5- to 10-picomole (submicrogram) level.
    • Demonstrated applicability to polypeptides of diverse sizes (less than 10 to over 1000 residues).
    • Direct analysis of polypeptides isolated from gel electrophoresis.

    Conclusions:

    • Automated microsequencing offers a highly sensitive approach for protein analysis.
    • The technique is versatile, accommodating a wide range of polypeptide sizes.
    • This method facilitates direct protein sequencing from gel-purified samples, advancing proteomic studies.