Abstract:
:Various animal models have been used for studies of bupivacaine cardiovascular toxicity. These studies are difficult to relate to the clinical situation, since the disposition of bupivacaine in the various species is unknown. The serum protein binding of bupivacaine, therefore, was determined in human, sheep, monkey, dog, and rat at physiologic pH using ultrafiltration. Since a mixed acidosis results during a systemic toxicity reaction to bupivacaine, the influences of an acidic pH, resulting from the addition of lactic acid, also was examined. All sera exhibited two classes of binding sites, a high-affinity, low-capacity class (class 1) and a low-affinity, high-capacity class (class 2). When compared to human serum at physiologic pH, a significantly higher (P less than 0.05) affinity constant for the class 1 sites was observed for all species studied, with the exception of the rat. All species studied exhibited a significantly lower (P less than 0.05) capacity for the class 1 sites. The binding parameters of the class 2 sites displayed no significant difference. An acid pH resulted in a decrease in bupivacaine protein binding over the entire concentration range studied for all species, with the exception of the monkey. Monkey serum exhibited no change in bupivacaine binding with a decrease in pH. Since protein binding explains only a portion of the total disposition of bupivacaine, further delineation of each animal model under both acidotic and physiologic conditions needs to be accomplished before the animal studies currently under investigation can be extrapolated to the clinical situation.
journal_name
Anesthesiologyjournal_title
Anesthesiologyauthors
Coyle DE,Denson DD,Thompson GA,Myers JA,Arthur GR,Bridenbaugh POdoi
10.1097/00000542-198408000-00003subject
Has Abstractpub_date
1984-08-01 00:00:00pages
127-33issue
2eissn
0003-3022issn
1528-1175journal_volume
61pub_type
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