title: Doxycycline binding to plasma albumin of several species.
abstract: The affinity of doxycycline for crystalline plasma albumin fraction V, originating from sheep, dogs, cats, cows, pigs and humans, was evaluated by means of double-reciprocal and Scatchard plots. Mathematical modelling and weighted least-squares non-linear regression analysis of each Scatchard plot identified one binding component characterized by one high affinity binding site, and a second component attributed to non-specific binding to albumin. Association constants for this binding site ranged from 38,471 +/- 13,369 (SEM) l/mol for the interaction of doxycycline with ovine albumin to 6405 +/- 2375 l/mol for the interaction of doxycycline with human albumin. Statistical evaluation of the results suggested slight species-related differences in the values of association constants. Diphenylhydantoin, phenobarbital or carbamazepine did not displace doxycycline from binding sites on bovine albumin.
authors: Department of Anatomy, Physiological Sciences, College of Veterinary Medicine, North Carolina State University, Raleigh 27606.
authors: J L
authors: JL
authors: Riond
authors: J E
authors: JE
authors: Riviere
mesh_terms: D000818:Animals; D002415:Cats / Q000097:blood; D002417:Cattle / Q000097:blood; D004285:Dogs / Q000097:blood; D004318:Doxycycline / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D012044:Regression Analysis; D012709:Serum Albumin / Q000378:metabolism*; D012756:Sheep / Q000097:blood; D012984:Software; D013552:Swine / Q000097:blood
chemical_list: D012709:Serum Albumin; D004318:Doxycycline