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Amidated carboxyl groups in elastin

H M Kagan, R M Lerch

    Biochimica Et Biophysica Acta
    |May 20, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Most dicarboxylic amino acids in elastin are amidated, influencing its apolar character and interactions. This amidation impacts elastase binding and hydrolysis, revealing key structural and functional insights into this connective tissue protein.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Connective Tissue Research

    Background:

    • Dicarboxylic amino acids in elastin are crucial for electrostatic interactions with elastase.
    • The ionization state of these residues at physiological pH is critical for protein function.

    Purpose of the Study:

    • To investigate the amidation of glutamic and aspartic acid residues in elastin.
    • To determine the functional implications of amidated dicarboxylic acid residues on elastase interaction and elastin structure.

    Main Methods:

    • Quantification of acid-labile amide-bound ammonia in elastin hydrolysates using glutamate dehydrogenase assay.
    • Amino acid analysis of esterified and reduced elastin to determine specific amidated residues.
    • Enzymatic assays with elastase on native and modified elastin, including the effect of sodium dodecyl sulfate.

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    Main Results:

    • Ligament elastin contains approximately 70% amidated dicarboxylic acid residues.
    • Elastin contains approximately 18 glutamine, 3 asparagine, 4 glutamic acid, and 5 aspartic acid residues per 1000 residues.
    • Amidated elastin derivatives showed reduced elastase substrate activity, which was restored by sodium dodecyl sulfate.

    Conclusions:

    • The majority of dicarboxylic amino acids in elastin exist as neutral amides, contributing to its apolar nature.
    • Amidation significantly influences elastin's interaction with elastase and its susceptibility to hydrolysis.
    • These findings have implications for elastin's metabolic stability, ligand binding, and overall structural integrity.