Literature DB >> 7381721

Serum protein binding alterations of selected cephalosporin antibiotics by fatty acids and their derivatives.

D H Pitkin, P Actor, J A Weisbach.   

Abstract

Saturated fatty acids containing 10--14 carbon atoms were more potent inhibitors of serum protein binding than those containing shorter or longer carbon chains. Introduction of unsaturation into chains containing 16 or 18 carbons increased their inhibitory potency. Triglycerides and fatty acid esters, chlorides, thiols, and amides had no inhibitory activity. When inhibition was observed, it was concentration dependent and occurred when the molar ratio of fatty acid to protein equaled or exceeded three. The change in percent serum protein binding in the presence of an effective inhibitor was the greatest with cephalosporins that were most highly bound in the absence of an inhibitor.

Entities:  

Mesh:

Substances:

Year:  1980        PMID: 7381721     DOI: 10.1002/jps.2600690330

Source DB:  PubMed          Journal:  J Pharm Sci        ISSN: 0022-3549            Impact factor:   3.534


  3 in total

Review 1.  Cefonicid. A review of its antibacterial activity, pharmacological properties and therapeutic use.

Authors:  E Saltiel; R N Brogden
Journal:  Drugs       Date:  1986-09       Impact factor: 9.546

2.  Effect of caffeine on ceftriaxone disposition and plasma protein binding in the rat.

Authors:  K I Kwon; D W Bourne
Journal:  J Pharmacokinet Biopharm       Date:  1986-08

3.  Ceftriaxone disposition in open-heart surgery patients.

Authors:  G L Jungbluth; M T Pasko; T R Beam; W J Jusko
Journal:  Antimicrob Agents Chemother       Date:  1989-06       Impact factor: 5.191

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.