Display options
Cite
Trnavská Z, Trnavský K. Characterization of salicylate binding to synovial fluid and plasma protein in patients with rheumatoid arthritis. Eur J Clin Pharmacol. 1980;18(5):403-6doi: 10.1007/BF00636793.
Trnavská, Z., & Trnavský, K. (1980). Characterization of salicylate binding to synovial fluid and plasma protein in patients with rheumatoid arthritis. European journal of clinical pharmacology, 18(5), 403-6. https://doi.org/10.1007/BF00636793
Trnavská, Z, and Trnavský, K. "Characterization of salicylate binding to synovial fluid and plasma protein in patients with rheumatoid arthritis." European journal of clinical pharmacology vol. 18,5 (1980): 403-6. doi: https://doi.org/10.1007/BF00636793
Trnavská Z, Trnavský K. Characterization of salicylate binding to synovial fluid and plasma protein in patients with rheumatoid arthritis. Eur J Clin Pharmacol. 1980 Nov;18(5):403-6. doi: 10.1007/BF00636793. PMID: 7439262.
Copy Download .nbib Format: NLM
Share it on
Full text links
Springer

Eur J Clin Pharmacol. 1980 Nov;18(5):403-6. doi: 10.1007/BF00636793.

Characterization of salicylate binding to synovial fluid and plasma protein in patients with rheumatoid arthritis.

European journal of clinical pharmacology

Z Trnavská, K Trnavský

PMID: 7439262 DOI: 10.1007/BF00636793

Abstract

Protein binding of salicylate in synovial fluid and plasma from patients with rheumatoid arthritis was studied by equilibrium dialysis. Protein binding in the synovial fluid was considerably lower at all salicylate concentrations studied (0.07 - 2.2 mM). Scatchard plots of the data were analyzed assuming binding to two classes of binding sites, each plasma sample being diluted to an albumin concentration equal to that in synovial fluid from the same patient. Binding to the primary binding sites was considerably decreased in synovial fluid in comparison with plasma. The affinity of the secondary binding sites was slightly lower. Thus, at a low therapeutic drug concentration, the decreased binding of salicylate to synovial fluid protein in patients with rheumatoid arthritis could mainly be accounted for by decreasing affinity of binding to the primary binding sites.

References

  1. Clin Pharmacokinet. 1978 Mar-Apr;3(2):144-54 - PubMed
  2. Eur J Clin Pharmacol. 1976 Feb 6;9(4):285-90 - PubMed
  3. Anal Biochem. 1972 Jul;48(1):80-9 - PubMed
  4. J Pharm Sci. 1975 Oct;64(10):1711-3 - PubMed
  5. Ann N Y Acad Sci. 1973 Nov 26;226:115-26 - PubMed
  6. J Pharmacol Exp Ther. 1971 Feb;176(2):261-72 - PubMed
  7. Anal Biochem. 1967 Sep;20(3):525-32 - PubMed
  8. Drug Metab Rev. 1979;9(1):3-19 - PubMed
  9. Agents Actions. 1979 Jun;9(2):212-6 - PubMed
  10. Biochem Pharmacol. 1974 Jun 15;23(12):1767-76 - PubMed
  11. Arthritis Rheum. 1964 Apr;7:103-9 - PubMed
  12. Bull Johns Hopkins Hosp. 1960 Nov;107:278-90 - PubMed
  13. J Pharmacokinet Biopharm. 1979 Apr;7(2):195-206 - PubMed
  14. Rev Rhum Mal Osteoartic. 1978 Mar;45(3):165-9 - PubMed
  15. Arthritis Rheum. 1967 Aug;10(4):348-51 - PubMed
  16. Drug Metab Rev. 1976;5(1):43-140 - PubMed
  17. N Engl J Med. 1976 Feb 5;294(6):311-6 - PubMed

Substances

MeSH terms

Publication Types

LinkOut - more resources