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Antibody buffering of systemically administered lysozyme *
Author(s) -
O’Hear Carol,
Foote Jefferson
Publication year - 2010
Publication title -
european journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0902-4441
DOI - 10.1111/j.1600-0609.2009.01383.x
Subject(s) - lysozyme , antibody , chemistry , dose , enzyme , pharmacokinetics , in vivo , pharmacology , biochemistry , immunology , medicine , biology , microbiology and biotechnology
Objective: To assess the ability of an anti‐lysozyme antibody to stabilize the plasma pharmacokinetics of lysozyme through a ‘buffering’ effect. Methods: Hen egg lysozyme was radiolabeled with 14 C and infused with or without the murine anti‐lysozyme antibody D1.3 into the jugular vein of rats. The dosages of antibody and lysozyme were varied, and the antibody and lysozyme were administered either together or in separate infusions. Results: Buffering of lysozyme with an equimolar amount of D1.3 more than doubled the plasma half‐life of lysozyme and addition of more antibody buffer prolonged the half‐life to an even greater extent. D1.3 bound lysozyme that was infused several minutes after the D1.3 administration, indicating that D1.3 can be charged with drug in vivo . Conclusion: Antibody buffering of monovalent therapeutic enzymes is possible and may have potential for clinical use.