[Determination of the protein binding of drugs by continuous ultrafiltration. 9. Comparison of the binding of nonsteroid antirheumatics to human serum albumin and their interaction with phenprocoumon]

Arch Pharm (Weinheim). 1989 Apr;322(4):241-3. doi: 10.1002/ardp.19893220410.
[Article in German]

Abstract

Binding to HSA has been determined for diflunisal (alpha = 0.03%), diclofenac (0.09), ibuprofen (0.10), bumadizone (0.11), ketoprofen (0.14), oxyphenbutazone (0.28), indomethacin (0.39), mofebutazone (0.57), tenoxicam (0.59), piroxicam (0.91), salicylic acid (1.00), o-carbamoylphenoxyacetic acid (11.58) and salicylamide (24.91). The free concentration of phenprocoumon was raised by diflunisal up to 35% in a dose dependent manner. Ibuprofen and piroxicam did not show significant effects. It is concluded that diflunisal is bound only slightly to the phenoprocoumon binding site of HSA while ibuprofen has no affinity to this part of the albumin molecule.

Publication types

  • Comparative Study
  • English Abstract

MeSH terms

  • 4-Hydroxycoumarins / blood*
  • Anti-Inflammatory Agents, Non-Steroidal / blood*
  • Binding, Competitive
  • Humans
  • Phenprocoumon / blood*
  • Protein Binding
  • Serum Albumin / metabolism*
  • Ultrafiltration

Substances

  • 4-Hydroxycoumarins
  • Anti-Inflammatory Agents, Non-Steroidal
  • Serum Albumin
  • Phenprocoumon