SEQUENCE DEPENDENT DEAMIDATION RATES FOR MODEL PEPTIDES OF HEN EGG‐WHITE LYSOZYME

Abstract
The rates of deamidation in pH 7.5, 0.15 M, 37°C potassium phosphate buffer of eleven pentapeptide models of the sequences found near asparaginyl and glutaminyl residues in egg white lysozyme were measured. These rates and rate estimates from previous measurements were used to calculate a sequence‐determined half‐life for non‐deamidated egg white lysozyme. Deamidation of the peptides during synthesis and purification was also measured. The implications of these measurements for biological deamidation and deamidation during peptide synthesis are discussed.

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