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Titration study of acetylated lysozyme.

T Okuda, S Sugai

    Journal of Biochemistry
    |December 1, 1975
    PubMed
    Summary

    This study investigates lysozyme

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Lysozyme (EC 3.2.1.17) is a crucial enzyme with complex interactions involving its carboxyl and amino groups.
    • Understanding these interactions is key to elucidating enzyme function and stability.
    • Identifying abnormal pK values of residues provides insights into the enzyme's microenvironment.

    Purpose of the Study:

    • To investigate the interaction between carboxyl and amino groups in native lysozyme.
    • To identify the specific positions and pK values of abnormal carboxyl groups.
    • To characterize the titratable residues in native and N-acetylated lysozyme.

    Main Methods:

    • Preparation of N-acetylated lysozyme to selectively modify amino groups.
    • pH titration of native and N-acetylated lysozyme in aqueous KCl solutions.
    • Spectrophotometric titration to assess tyrosine residue titratability.

    Main Results:

    • Acetylation modified six amino groups, leaving Lys 33 as the sole titratable amino group.
    • pH titration revealed fewer titratable groups in acetylated lysozyme, with abnormal carboxyl groups identified at Asp 48, Asp 66, and Asp 87.
    • Spectrophotometric titration showed all three tyrosine residues are titratable in acetylated lysozyme, with Tyr 20 being untitratable in native lysozyme within the pH range of 8-12.6.

    Conclusions:

    • Specific carboxyl groups (Asp 48, 66, 87) exhibit abnormal pK values in native lysozyme due to interactions with other residues.
    • Lys 33 is the primary titratable amino group in N-acetylated lysozyme.
    • Tyr 20's untitratability in native lysozyme suggests a unique microenvironment influencing its ionization.

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