By Eugene J. McNally, Eugene McNally, Jayne E. Hastedt

Preformulation and the improvement of conventional options and lyophilized formulations often used for intravenous supply and non-traditional formulations also are addressed. simply because many advancements within the box have emerged because the book of the 1st variation, this moment variation addresses very important new patient-friendly advancements within the box, comparable to formula for implantable units, needle-free formula and supply techniques, and oral supply of proteins.

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Capasso (58) proposed the extrathermodynamic relationship shown in Equation 1: Log k1 = Xp + ZAsn + Yp (1) Here k1 is the observed rate constant for deamidation, Xp is the average contribution of the specific amino acid that precedes Asn, Yp is the average contribution due to the amino acid that follows Asn, and ZAsn is the value when both the preceding and following amino acids are glycine. Over 60 peptides were included in the database. As expected, the greatest influence on the deamidation rate in peptides was found to arise from the identity of the following amino acid.

Proline Hydroxyl radical oxidation by the hydroxyl radical of proline (144,145), as well as glutamic acid and aspartic acid (146), is characterized by site-specific cleavage of the polypeptide chain on the C-terminal end of the residue. Formulation Factors and Oxidation Overview of Excipient Effects Shown in Table 2 is a list of first-order rate constants for the reaction of OH with selected formulation excipients that have proved useful in protein systems (101). As with the amino acids shown in Table 1, the rate constants of the excipients listed in Table 2 vary by up to three orders of magnitude.

J Biol Chem 1991; 266:22549–22556. 13. Tomizawa H, Yamada H, Wada K, Imoto T. Stabilization of lysozyme against irreversible inactivation by suppression of chemical reactions. J Biochem 1995; 117:635–639. 14. Zhao M, Bada JL, Ahern TJ. Racemization rates of asparagine-aspartic acid residues in lysozyme at 100°C as a function of pH. Bioorg Chem 1989; 17:36–40. 15. De Boni S, Oberthür C, Hamburger M, Scriba GKE. Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry.

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